NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16130302|ref|NP_416871|]
View 

sensor histidine kinase EvgS [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

acid-sensing system histidine kinase EvgS( domain architecture ID 11484536)

acid-sensing system histidine kinase EvgS phosphorylates EvgA via a four-step phosphorelay in response to environmental signals

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
1-1197 0e+00

acid-sensing system histidine kinase EvgS;


:

Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 2407.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     1 MKFLPYIFLLCCGLWSTISFADEDYIEYRGISSNNRVTLDPLRLSNKELRWLASKKNLVIAVHKSQTATLLHTDSQQRVR 80
Cdd:PRK09959    1 MKFLPYIFLLCCGLWSTISFADEDYIEYRGISSNNRVTLDPLRLSNKELRWLASKKNLVIAVHKSQTATLLHTDSQQRVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    81 GINADYLNLLKRALNIKLTLREYADHQKAMDALAEGEVDIVLSHLVTSPPLNNDIAATKPLIITFPALVTTLHDSMRPLT 160
Cdd:PRK09959   81 GINADYLNLLKRALNIKLTLREYADHQKAMDALEEGEVDIVLSHLVASPPLNDDIAATKPLIITFPALVTTLHDSMRPLT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   161 SPKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSLNVVKYYNSPRQY 240
Cdd:PRK09959  161 SSKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGQNDYFIGSNIITSSMISRYFTHSLNVVKYYNSPRQY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   241 NFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPNLKVLENPYSPPYSMTDE 320
Cdd:PRK09959  241 NFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPDLKVLENPYSPPYSMTDE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   321 NGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLSPGGWDIIPGAIYSEDRENNVLFAEAFITTPYVFVMQKAPDS 400
Cdd:PRK09959  321 NGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLNPGGWDIIPGAIYSEDRENNVLFAEAFITTPYVFVMQKAPDS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   401 EQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRYMIDHYYPNELYHFLIPGVP 480
Cdd:PRK09959  401 EQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIKVDNASAAFHKVKEGELDALVATQLNSRYMIDHYYPNELYHFLIPGVP 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   481 NASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWIKMPNVTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRS 560
Cdd:PRK09959  481 NASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWIKMPNVTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRS 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   561 VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLENSDSPFKDVFSNAHEVTA 640
Cdd:PRK09959  561 VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLENSDSPFKDVFSNAHEVTA 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   641 ETKENRTIYTQVFEIDNGIEKRCINHWHTLCNLPASDNAVYICGWQDITETRDLINALEVEKNKAIKATVAKSQFLATMS 720
Cdd:PRK09959  641 ETKENRTIYTQVFEIDNGIEKRCINHWHTLCNLPASDHAVYICGWQDITETRDLIHALEVERNKAINATVAKSQFLATMS 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   721 HEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFG 800
Cdd:PRK09959  721 HEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFG 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   801 AIAASKSIALSCSSTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEE 880
Cdd:PRK09959  801 AIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEE 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   881 QQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLS 960
Cdd:PRK09959  881 QQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLS 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHETHKDLPAA 1120
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHETHKDLPAA 1120
                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302  1121 FQALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEITPVSDDSKPEILQLLNSVKEHIAELDQEIAVFCQKND 1197
Cdd:PRK09959 1121 FHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEITPVSDDSKPEILQLLNSVKEHIAELDQEIAVFCQKND 1197
 
Name Accession Description Interval E-value
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
1-1197 0e+00

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 2407.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     1 MKFLPYIFLLCCGLWSTISFADEDYIEYRGISSNNRVTLDPLRLSNKELRWLASKKNLVIAVHKSQTATLLHTDSQQRVR 80
Cdd:PRK09959    1 MKFLPYIFLLCCGLWSTISFADEDYIEYRGISSNNRVTLDPLRLSNKELRWLASKKNLVIAVHKSQTATLLHTDSQQRVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    81 GINADYLNLLKRALNIKLTLREYADHQKAMDALAEGEVDIVLSHLVTSPPLNNDIAATKPLIITFPALVTTLHDSMRPLT 160
Cdd:PRK09959   81 GINADYLNLLKRALNIKLTLREYADHQKAMDALEEGEVDIVLSHLVASPPLNDDIAATKPLIITFPALVTTLHDSMRPLT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   161 SPKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSLNVVKYYNSPRQY 240
Cdd:PRK09959  161 SSKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGQNDYFIGSNIITSSMISRYFTHSLNVVKYYNSPRQY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   241 NFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPNLKVLENPYSPPYSMTDE 320
Cdd:PRK09959  241 NFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPDLKVLENPYSPPYSMTDE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   321 NGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLSPGGWDIIPGAIYSEDRENNVLFAEAFITTPYVFVMQKAPDS 400
Cdd:PRK09959  321 NGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLNPGGWDIIPGAIYSEDRENNVLFAEAFITTPYVFVMQKAPDS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   401 EQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRYMIDHYYPNELYHFLIPGVP 480
Cdd:PRK09959  401 EQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIKVDNASAAFHKVKEGELDALVATQLNSRYMIDHYYPNELYHFLIPGVP 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   481 NASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWIKMPNVTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRS 560
Cdd:PRK09959  481 NASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWIKMPNVTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRS 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   561 VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLENSDSPFKDVFSNAHEVTA 640
Cdd:PRK09959  561 VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLENSDSPFKDVFSNAHEVTA 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   641 ETKENRTIYTQVFEIDNGIEKRCINHWHTLCNLPASDNAVYICGWQDITETRDLINALEVEKNKAIKATVAKSQFLATMS 720
Cdd:PRK09959  641 ETKENRTIYTQVFEIDNGIEKRCINHWHTLCNLPASDHAVYICGWQDITETRDLIHALEVERNKAINATVAKSQFLATMS 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   721 HEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFG 800
Cdd:PRK09959  721 HEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFG 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   801 AIAASKSIALSCSSTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEE 880
Cdd:PRK09959  801 AIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEE 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   881 QQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLS 960
Cdd:PRK09959  881 QQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLS 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHETHKDLPAA 1120
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHETHKDLPAA 1120
                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302  1121 FQALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEITPVSDDSKPEILQLLNSVKEHIAELDQEIAVFCQKND 1197
Cdd:PRK09959 1121 FHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEITPVSDDSKPEILQLLNSVKEHIAELDQEIAVFCQKND 1197
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
301-519 1.24e-83

The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270425 [Multi-domain]  Cd Length: 221  Bit Score: 271.40  E-value: 1.24e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  301 HPNLKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLSPGGWDIIPGAIYSEDRENNVL 380
Cdd:cd13707    1 HPVVRVVVNPDLAPLSFFDSNGQFRGISADLLELISLRTGLRFEVVRASSPAEMIEALRSGEADMIAALTPSPEREDFLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  381 FAEAFITTPYVFVMQKAPDSEQTLK--KGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLN 458
Cdd:cd13707   81 FTRPYLTSPFVLVTRKDAAAPSSLEdlAGKRVAIPAGSALEDLLRRRYPQIELVEVDNTAEALALVASGKADATVASLIS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302  459 SRYMIDHYYPNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWI 519
Cdd:cd13707  161 ARYLINHYFRDRLKIAGILGEPPAPIAFAVRRDQPELLSILDKALLSIPPDELLELRNRWR 221
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
697-937 3.84e-67

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 225.94  E-value: 3.84e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  697 ALEVEKNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELL-SGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIE 775
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLlDEEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  776 SGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSsTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEG-AVKITTs 854
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELD-LPPELPLVYADPELLEQVLANLLDNAIKYSPPGgTITISA- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  855 lgHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI 934
Cdd:COG2205  159 --RREGDGVRI--SVSDNGPGIPEEELERIFERFYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234

                 ...
gi 16130302  935 PVE 937
Cdd:COG2205  235 PLA 237
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
686-1187 3.94e-67

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 245.46  E-value: 3.94e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    686 QDITETRDLINALEVEKNKAI----KATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYaTGQSL 761
Cdd:TIGR02956  434 QELAETNERLNAEVKNHAKARaeaeEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINR-SGESL 512
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    762 LGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC--SSTFPEHYLvkIDPQAFKQVLSNLLSN 839
Cdd:TIGR02956  513 LDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLniPEQLPNWWQ--GDGPRIRQVLINLVGN 590
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    840 ALKFTTEGAVKITTSLghIDDNHAVIKMTimDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLS 919
Cdd:TIGR02956  591 AIKFTDRGSVVLRVSL--NDDSSLLFEVE--DTGCGIAEEEQATLFDAFTQADGRRRSGGTGLGLAISQRLVEAMDGELG 666
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    920 LESHPGIGTTFTITIPVEISQQVATveAKAEQPITLPeKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVS 999
Cdd:TIGR02956  667 VESELGVGSCFWFTLPLTRGKPAED--SATLTVIDLP-PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFH 743
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   1000 MQHYDLLITDVNMPNMDGFELTRKLRE---QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQ- 1075
Cdd:TIGR02956  744 QHAFDLALLDINLPDGDGVTLLQQLRAiygAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAg 823
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   1076 --------VAHIAPQYRHLDIEALKNNT------------------ANDLQL-----MQEILMTFQHETHKDLPAAFQAL 1124
Cdd:TIGR02956  824 gksnteapVLSASPSFDSASVIENAQADdipesnqaseflldeeqlQQDIEVlgvekVRQLVALFKTSSAEQLEELSAAR 903
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130302   1125 EAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEI-TPVSDDSKPEILQLLNSVKEHIAELDQ 1187
Cdd:TIGR02956  904 AVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKqGKTGALELSDIDEIKQAWQASKTALDQ 967
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
303-519 2.99e-39

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 145.55  E-value: 2.99e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     303 NLKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSpITVSHNIHAGTQLSPGGWDIIPGAI-YSEDRENNVLF 381
Cdd:smart00062    1 TLRVGTNGDYPPFSFADEDGELTGFDVDLAKAIAKELGLKVE-FVEVSFDSLLTALKSGKIDVVAAGMtITPERAKQVDF 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     382 AEAFITTPYVFVMQKAPD--SEQTL--KKGMKVAIPYYYELhsqLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQL 457
Cdd:smart00062   80 SDPYYRSGQVILVRKDSPikSLEDLkgKKVAVVAGTTAEEL---LKKLYPEAKIVSYDSNAEALAALKAGRADAAVADAP 156
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130302     458 nSRYMIDHYYPNELYHFLIPGVPN-ASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKWI 519
Cdd:smart00062  157 -LLAALVKQHGLPELKIVPDPLDTpEGYAIAVRKGDPELLDKINKALKELKADGTLkKISEKWF 219
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
961-1070 5.18e-33

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 123.42  E-value: 5.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 16130302   1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
Cdd:pfam00072   81 DEDDAVEALEAGADDFLSKPFDPDELLAAI 110
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
712-935 3.00e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 98.36  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   712 KSQFLATMSHEIRTPISSIMGFLELLSgSGLSKEQRVEAISLAYATGQsLLGLIGEILDVDKIESGN--YQLQPqwVDIP 789
Cdd:NF012163  240 RRDFMADISHELRTPLAVLRAELEAIQ-DGIRKFTPESLDSLQAEVGT-LTKLVDDLHDLSMSDEGAlaYQKAS--VDLV 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   790 TLVQNTCHSFGAIAASKSIALSCSstFPEHYLVKIDPQAFKQVLSNLLSNALKFT-TEGAVKITTSlghidDNHAVIKMT 868
Cdd:NF012163  316 PLLEVEGGAFRERFASAGLELEVS--LPDSSLVFGDRDRLMQLFNNLLENSLRYTdSGGSLHISAS-----QRPKEVTLT 388
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130302   869 IMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:NF012163  389 VADSAPGVSDEQLARLFERFYRVevSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
 
Name Accession Description Interval E-value
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
1-1197 0e+00

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 2407.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     1 MKFLPYIFLLCCGLWSTISFADEDYIEYRGISSNNRVTLDPLRLSNKELRWLASKKNLVIAVHKSQTATLLHTDSQQRVR 80
Cdd:PRK09959    1 MKFLPYIFLLCCGLWSTISFADEDYIEYRGISSNNRVTLDPLRLSNKELRWLASKKNLVIAVHKSQTATLLHTDSQQRVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    81 GINADYLNLLKRALNIKLTLREYADHQKAMDALAEGEVDIVLSHLVTSPPLNNDIAATKPLIITFPALVTTLHDSMRPLT 160
Cdd:PRK09959   81 GINADYLNLLKRALNIKLTLREYADHQKAMDALEEGEVDIVLSHLVASPPLNDDIAATKPLIITFPALVTTLHDSMRPLT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   161 SPKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSLNVVKYYNSPRQY 240
Cdd:PRK09959  161 SSKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGQNDYFIGSNIITSSMISRYFTHSLNVVKYYNSPRQY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   241 NFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPNLKVLENPYSPPYSMTDE 320
Cdd:PRK09959  241 NFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWLDTGNLAFLNKPLELTEHEKQWIKQHPDLKVLENPYSPPYSMTDE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   321 NGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLSPGGWDIIPGAIYSEDRENNVLFAEAFITTPYVFVMQKAPDS 400
Cdd:PRK09959  321 NGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLNPGGWDIIPGAIYSEDRENNVLFAEAFITTPYVFVMQKAPDS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   401 EQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRYMIDHYYPNELYHFLIPGVP 480
Cdd:PRK09959  401 EQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIKVDNASAAFHKVKEGELDALVATQLNSRYMIDHYYPNELYHFLIPGVP 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   481 NASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWIKMPNVTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRS 560
Cdd:PRK09959  481 NASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWIKMPNVTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRS 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   561 VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLENSDSPFKDVFSNAHEVTA 640
Cdd:PRK09959  561 VRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLENSDSPFKDVFSNAHEVTA 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   641 ETKENRTIYTQVFEIDNGIEKRCINHWHTLCNLPASDNAVYICGWQDITETRDLINALEVEKNKAIKATVAKSQFLATMS 720
Cdd:PRK09959  641 ETKENRTIYTQVFEIDNGIEKRCINHWHTLCNLPASDHAVYICGWQDITETRDLIHALEVERNKAINATVAKSQFLATMS 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   721 HEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFG 800
Cdd:PRK09959  721 HEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFG 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   801 AIAASKSIALSCSSTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEE 880
Cdd:PRK09959  801 AIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEE 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   881 QQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLS 960
Cdd:PRK09959  881 QQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLS 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:PRK09959  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHETHKDLPAA 1120
Cdd:PRK09959 1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDIEALKNNTANDLQLMQEILMTFQHETHKDLPAA 1120
                        1130      1140      1150      1160      1170      1180      1190
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302  1121 FQALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEITPVSDDSKPEILQLLNSVKEHIAELDQEIAVFCQKND 1197
Cdd:PRK09959 1121 FHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEITPVSDDSKPEILQLLNSVKEHIAELDQEIAVFCQKND 1197
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
301-519 1.24e-83

The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270425 [Multi-domain]  Cd Length: 221  Bit Score: 271.40  E-value: 1.24e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  301 HPNLKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLSPGGWDIIPGAIYSEDRENNVL 380
Cdd:cd13707    1 HPVVRVVVNPDLAPLSFFDSNGQFRGISADLLELISLRTGLRFEVVRASSPAEMIEALRSGEADMIAALTPSPEREDFLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  381 FAEAFITTPYVFVMQKAPDSEQTLK--KGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLN 458
Cdd:cd13707   81 FTRPYLTSPFVLVTRKDAAAPSSLEdlAGKRVAIPAGSALEDLLRRRYPQIELVEVDNTAEALALVASGKADATVASLIS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302  459 SRYMIDHYYPNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWI 519
Cdd:cd13707  161 ARYLINHYFRDRLKIAGILGEPPAPIAFAVRRDQPELLSILDKALLSIPPDELLELRNRWR 221
PBP2_BvgS_D1 cd13705
The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
55-275 9.54e-71

The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270423 [Multi-domain]  Cd Length: 221  Bit Score: 235.56  E-value: 9.54e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   55 KKNLVIAVHKSQTATLLHTDSQQRVRGINADYLNLLKRALNIKLTLREYADHQKAMDALAEGEVDIVLSHLvTSPPLNND 134
Cdd:cd13705    1 KRTLRVGVSAPDYPPFDITSSGGRYEGITADYLGLIADALGVRVEVRRYPDREAALEALRNGEIDLLGTAN-GSEAGDGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  135 IAATKPLIITFPALVTTLHDSMRPLTSPKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNI 214
Cdd:cd13705   80 LLLSQPYLPDQPVLVTRIGDSRQPPPDLAGKRVAVVPGYLPAEEIKQAYPDARIVLYPSPLQALAAVAFGQADYFLGDAI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302  215 ITSSMISRYFTHSLNVVKYYNSPRQYNFFLTRKESVILNEVLNRFVDALTNEVRYEVSQNW 275
Cdd:cd13705  160 SANYLISRNYLNNLRIVRFAPLPSRGFGFAVRPDNTRLLRLLNRALAAIPDEQRDEILRRW 220
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
697-937 3.84e-67

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 225.94  E-value: 3.84e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  697 ALEVEKNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELL-SGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIE 775
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLlDEEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  776 SGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSsTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEG-AVKITTs 854
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELD-LPPELPLVYADPELLEQVLANLLDNAIKYSPPGgTITISA- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  855 lgHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI 934
Cdd:COG2205  159 --RREGDGVRI--SVSDNGPGIPEEELERIFERFYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234

                 ...
gi 16130302  935 PVE 937
Cdd:COG2205  235 PLA 237
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
686-1187 3.94e-67

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 245.46  E-value: 3.94e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    686 QDITETRDLINALEVEKNKAI----KATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYaTGQSL 761
Cdd:TIGR02956  434 QELAETNERLNAEVKNHAKARaeaeEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINR-SGESL 512
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    762 LGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC--SSTFPEHYLvkIDPQAFKQVLSNLLSN 839
Cdd:TIGR02956  513 LDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLniPEQLPNWWQ--GDGPRIRQVLINLVGN 590
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    840 ALKFTTEGAVKITTSLghIDDNHAVIKMTimDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLS 919
Cdd:TIGR02956  591 AIKFTDRGSVVLRVSL--NDDSSLLFEVE--DTGCGIAEEEQATLFDAFTQADGRRRSGGTGLGLAISQRLVEAMDGELG 666
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    920 LESHPGIGTTFTITIPVEISQQVATveAKAEQPITLPeKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVS 999
Cdd:TIGR02956  667 VESELGVGSCFWFTLPLTRGKPAED--SATLTVIDLP-PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFH 743
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   1000 MQHYDLLITDVNMPNMDGFELTRKLRE---QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQ- 1075
Cdd:TIGR02956  744 QHAFDLALLDINLPDGDGVTLLQQLRAiygAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAg 823
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   1076 --------VAHIAPQYRHLDIEALKNNT------------------ANDLQL-----MQEILMTFQHETHKDLPAAFQAL 1124
Cdd:TIGR02956  824 gksnteapVLSASPSFDSASVIENAQADdipesnqaseflldeeqlQQDIEVlgvekVRQLVALFKTSSAEQLEELSAAR 903
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130302   1125 EAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEI-TPVSDDSKPEILQLLNSVKEHIAELDQ 1187
Cdd:TIGR02956  904 AVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKqGKTGALELSDIDEIKQAWQASKTALDQ 967
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
685-937 3.09e-66

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 227.10  E-value: 3.09e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  685 WQDITETRDLINALEVEKNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELLSgSGLSKEQRvEAISLAYATGQSLLGL 764
Cdd:COG0642   83 LLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLL-EELDEEQR-EYLETILRSADRLLRL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  765 IGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPEHYLVKIDPQAFKQVLSNLLSNALKFT 844
Cdd:COG0642  161 INDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLP-DDLPTVRGDPDRLRQVLLNLLSNAIKYT 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  845 TEG-AVKITTSlghIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESH 923
Cdd:COG0642  240 PEGgTVTVSVR---REGDRVRI--SVEDTGPGIPPEDLERIFEPFFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESE 314
                        250
                 ....*....|....
gi 16130302  924 PGIGTTFTITIPVE 937
Cdd:COG0642  315 PGKGTTFTVTLPLA 328
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
703-1071 2.13e-63

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 233.71  E-value: 2.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   703 NKAIKATVAKSQFLATMSHEIRTPISSIMGFLELLSgsglSKEQRVEAISLAYATGQS---LLGLIGEILDVDKIESGny 779
Cdd:PRK10841  438 QAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQ----TKELPKGVDRLVTAMNNSsslLLKIISDILDFSKIESE-- 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   780 QLQ-------PQWVdIPTLVQNtchsFGAIAASKSIALSCsstFPEHYLVKI---DPQAFKQVLSNLLSNALKFTTEGAV 849
Cdd:PRK10841  512 QLKieprefsPREV-INHITAN----YLPLVVKKRLGLYC---FIEPDVPVAlngDPMRLQQVISNLLSNAIKFTDTGCI 583
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   850 KITTSlghIDDNHAVIKmtIMDSGSGLSQEEQQQLFKRYSQTSAGRQQT--GSGLGLMICKELIKNMQGDLSLESHPGIG 927
Cdd:PRK10841  584 VLHVR---VDGDYLSFR--VRDTGVGIPAKEVVRLFDPFFQVGTGVQRNfqGTGLGLAICEKLINMMDGDISVDSEPGMG 658
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   928 TTFTITIPVEISQQVATVEAKAEQ-------------------------------------------------------- 951
Cdd:PRK10841  659 SQFTIRIPLYGAQYPQKKGVEGLQgkrcwlavrnasleqfletllqrsgiqvqryegqeptpedvlitddpvqkkwqgra 738
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   952 --------------------------PITLP------------------------------EKLSILIADDHPTNRLLLK 975
Cdd:PRK10841  739 vitfcrrhigipleiapgewvhstatPHELPallariyrielesddsanalpstdkavsdnDDMMILVVDDHPINRRLLA 818
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   976 RQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNL 1055
Cdd:PRK10841  819 DQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANALAEEKQRCLEAGMDS 898
                         490
                  ....*....|....*.
gi 16130302  1056 CLFKPLTLDVLKTHLS 1071
Cdd:PRK10841  899 CLSKPVTLDVLKQTLT 914
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
686-937 2.58e-61

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 215.19  E-value: 2.58e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  686 QDITETRDLINAleveknkaikatvaKSQFLATMSHEIRTPISSIMGFLELL-SGSGLSKEQRVEAISLAYATGQSLLGL 764
Cdd:COG5002  153 RDITELERLEQM--------------RREFVANVSHELRTPLTSIRGYLELLlDGAADDPEERREYLEIILEEAERLSRL 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  765 IGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPEHYLVKIDPQAFKQVLSNLLSNALKFT 844
Cdd:COG5002  219 VNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLP-EDPLLVLGDPDRLEQVLTNLLDNAIKYT 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  845 TEGAvKITTSLgHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLES 922
Cdd:COG5002  298 PEGG-TITVSL-REEDDQVRI--SVRDTGIGIPEEDLPRIFERFYRVdkSRSRETGGTGLGLAIVKHIVEAHGGRIWVES 373
                        250
                 ....*....|....*
gi 16130302  923 HPGIGTTFTITIPVE 937
Cdd:COG5002  374 EPGKGTTFTITLPLA 388
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
557-1189 4.91e-61

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 224.43  E-value: 4.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   557 LLRSVRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEhyftadyyknaMLPLENSD-----SPfKDV 631
Cdd:PRK11091  136 LKNEIKEREETQIELEQQSSLLRSFLDASPDLVYYRNEDGEFSGCNRAME-----------LLTGKSEKqliglTP-KDV 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   632 FSN--AHEVtAETKEN--RT----IYTQVFEIDNGiEKRCINhwhtLCNLP-ASDNAVYI--CGW-QDITETRDLINALE 699
Cdd:PRK11091  204 YSPeaAEKV-IETDEKvfRHnvslTYEQWLDYPDG-RKACFE----LRKVPfYDRVGKRHglMGFgRDITERKRYQDALE 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   700 veknkaiKATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQR-------VEAISLayatgqsllGLI-GEILDV 771
Cdd:PRK11091  278 -------KASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRkylktihVSAITL---------GNIfNDIIDM 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   772 DKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKI 851
Cdd:PRK11091  342 DKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTV 421
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   852 TTSLghidDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ---TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGT 928
Cdd:PRK11091  422 RVRY----EEGDMLTFEVEDSGIGIPEDELDKIFAMYYQvkdSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGS 497
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   929 TFTITIPVEISQQVATvEAKAEQPITLPeKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLIT 1008
Cdd:PRK11091  498 CFTLTIHAPAVAEEVE-DAFDEDDMPLP-ALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLL 575
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1009 DVNMPNMDGFELTRKLREQ--NSSL-PIWGLTANAQANEREKgLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRH 1085
Cdd:PRK11091  576 DIQLPDMTGLDIARELRERypREDLpPLVALTANVLKDKKEY-LDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVT 654
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1086 LDIEALKNNTANDLQLMQEILMTFQHETHKDLPAAFQ------------ALEAGDNRTFHQCIHRIHGAANILNLQKLIN 1153
Cdd:PRK11091  655 TEESSKANEALLDIPMLEQYVELVGPKLITDSLAVFEkmmpgylsvldsNLTARDQKGIVEEAHKIKGAAGSVGLRHLQQ 734
                         650       660       670
                  ....*....|....*....|....*....|....*...
gi 16130302  1154 ISHQLEIT--PVSDDskpeilqllnSVKEHIAELDQEI 1189
Cdd:PRK11091  735 LAQQIQSPdlPAWWD----------NVQDWVEELKNEW 762
PRK15347 PRK15347
two component system sensor kinase;
697-1159 1.55e-58

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 218.74  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   697 ALEVEKNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIES 776
Cdd:PRK15347  383 ALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQM-DLADTARQCTLSLLAIINNLLDFSRIES 461
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   777 GNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC--SSTFPEhYLvKIDPQAFKQVLSNLLSNALKFTTEGAVKITts 854
Cdd:PRK15347  462 GQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTfvGAHVPL-YL-HLDSLRLRQILVNLLGNAVKFTETGGIRLR-- 537
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   855 lGHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRQqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI 934
Cdd:PRK15347  538 -VKRHEQQLCF--TVEDTGCGIDIQQQQQIFTPFYQADTHSQ--GTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVL 612
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   935 PVE-----------------------------------------------------ISQQVATVEAKAEQPI-TLPEKLS 960
Cdd:PRK15347  613 PLNeyappeplkgelsaplalhrqlsawgitcqpghqnpalldpelaylpgrlydlLQQIIQGAPNEPVINLpLQPWQLQ 692
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLRE----QNSSLPIWGL 1036
Cdd:PRK15347  693 ILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDdpnnLDPDCMIVAL 772
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1037 TANAQANEREKGLSCGMNLCLFKPLTldvlkthLSQLHQVAHIAPQYRHL-DIEaLKNNTANDLQLMQEILMTFQHETHK 1115
Cdd:PRK15347  773 TANAAPEEIHRCKKAGMNHYLTKPVT-------LAQLARALELAAEYQLLrGIE-LSPQDSSCSPLLDTDDMALNSKLYQ 844
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 16130302  1116 DL----PAAFQALEAGDnrTFHQCIHRIHGAANILNLQKLINISHQLE 1159
Cdd:PRK15347  845 SLllllAQIEQAVENQE--VLSQLLHTLKGCAGQAGLTELQCAVIDLE 890
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
691-1175 1.90e-49

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 190.83  E-value: 1.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   691 TRDLINALE------VE----KNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQR--VEAISLAyATg 758
Cdd:PRK11107  262 TSDLRETLEqmeiqnVEldlaKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRdyLQTIERS-AN- 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   759 qSLLGLIGEILDVDKIESGNYQLQpqwvDIPTLVQNT--------CHSfgaiAASKSIALS--CSSTFPEHylVKIDPQA 828
Cdd:PRK11107  340 -NLLAIINDILDFSKLEAGKLVLE----NIPFSLRETldevvtllAHS----AHEKGLELTlnIDPDVPDN--VIGDPLR 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   829 FKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMI 906
Cdd:PRK11107  409 LQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQadASISRRHGGTGLGLVI 488
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   907 CKELIKNMQGDLSLESHPGIGTTFTITIPVEISQ---------------QVATVE------------------------- 946
Cdd:PRK11107  489 TQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPnpiidglptdclagkRLLYVEpnsaaaqatldilsetplevtyspt 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   947 --------------------------------------------------AKAEQ------------PITLPEKLSILIA 964
Cdd:PRK11107  569 lsqlpeahydilllglpvtfrepltmlherlakaksmtdflilalpcheqVLAEQlkqdgadaclskPLSHTRLLPALLE 648
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   965 -------------------------DDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFE 1019
Cdd:PRK11107  649 pchhkqppllpptdesrlpltvmavDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIR 728
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1020 LTRKLRE--QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLK---THLSQLHQVAHIAPQYRHLDIEALKNN 1094
Cdd:PRK11107  729 ACELIRQlpHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKqvlLRYKPGPKFTSRVVAPEPPEPVHFPNA 808
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1095 TAN------------DLQL-MQEILMTFQHETHKDLPaafQALEAGDNRTFHQCIHRIHGAA---NILNLQKL-INISHQ 1157
Cdd:PRK11107  809 TLDwqlalrqaagkpDLARdMLQMLLDFLPEVRNKVE---EALAGEDPEGLLDLIHKLHGSCsysGVPRLKKLcQLIEQQ 885
                         650
                  ....*....|....*...
gi 16130302  1158 LEITPVSDDSKPEILQLL 1175
Cdd:PRK11107  886 LRSGTSVEDLEPELLELL 903
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
829-936 9.33e-47

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 162.66  E-value: 9.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  829 FKQVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMI 906
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQadSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 16130302  907 CKELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
695-1190 2.04e-46

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 181.26  E-value: 2.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   695 INALEVE----KNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQR--VEAISlayATGQSLLGLIGEI 768
Cdd:PRK11466  423 LQELVIEhrqaRAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRddLRAIT---DSGESLLTILNDI 499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   769 LDVDKIESG--NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTE 846
Cdd:PRK11466  500 LDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDE 579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   847 GAVKITTSlghIDDNHAVIKmtIMDSGSGLSQEEQQQLFKRYSQTSAGRqqTGSGLGLMICKELIKNMQGDLSLESHPGI 926
Cdd:PRK11466  580 GSIVLRSR---TDGEQWLVE--VEDSGCGIDPAKLAEIFQPFVQVSGKR--GGTGLGLTISSRLAQAMGGELSATSTPEV 652
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   927 GTTFTITIPVEISqqVATVEAKAEQPITLpEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSM-QHYDL 1005
Cdd:PRK11466  653 GSCFCLRLPLRVA--TAPVPKTVNQAVRL-DGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNsEPFAA 729
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1006 LITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA---QANEREKGLSCGMnlcLFKPLTLDVLKTHLSQLHQVA-HIAp 1081
Cdd:PRK11466  730 ALVDFDLPDYDGITLARQLAQQYPSLVLIGFSAHVideTLRQRTSSLFRGI---IPKPVPREVLGQLLAHYLQLQvNND- 805
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  1082 qyRHLDIEALknntANDLQLM-----QEILMTFQHETHKDLPAAFQALEAGDNRTFHQCIHRIHGAANILNLQKLINISH 1156
Cdd:PRK11466  806 --QPLDVSQL----NEDAALMgtekiHEWLALFKQHALPLLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQACA 879
                         490       500       510
                  ....*....|....*....|....*....|....
gi 16130302  1157 QLEITPVSDDSKPEIlqllnsVKEHIAELDQEIA 1190
Cdd:PRK11466  880 QLEQQPLSAPLPHEE------ITRSVAALEAWLA 907
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
301-519 9.43e-46

The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 164.24  E-value: 9.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  301 HPNLKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSHNIHAGTQLSPGGWDIIPGAIYSEDRENNVL 380
Cdd:cd01007    1 HPVIRVGVDPDWPPFEFIDEGGEPQGIAADYLKLIAKKLGLKFEYVPGDSWSELLEALKAGEIDLLSSVSKTPEREKYLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  381 FAEAFITTPYVFVMQKAPDSEQTLK--KGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLN 458
Cdd:cd01007   81 FTKPYLSSPLVIVTRKDAPFINSLSdlAGKRVAVVKGYALEELLRERYPNINLVEVDSTEEALEAVASGEADAYIGNLAV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302  459 SRYMIDHYYPNELyHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWI 519
Cdd:cd01007  161 ASYLIQKYGLSNL-KIAGLTDYPQDLSFAVRKDWPELLSILNKALASISPEERQAIRNKWL 220
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
532-942 8.26e-42

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 160.91  E-value: 8.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  532 YSEQFYIVTTLSVLLVGSSLLWGFYL-LRSVRRRKVIQGDL-ENQISFRKALSDSlPNPTYVVNWQGNVISHNSAFEHYF 609
Cdd:COG5809   96 NGKRLEFSSKLSPIFDQNGDIEGMLAiSRDITERKRMEEALrESEEKFRLIFNHS-PDGIIVTDLDGRIIYANPAACKLL 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  610 TADY--YKNAML-------PLENSDSPFKDVFSNAHEVTAE----TKENRTIYtqvFEID-NGIEKRCINHWhtlcnlpa 675
Cdd:COG5809  175 GISIeeLIGKSIlelihsdDQENVAAFISQLLKDGGIAQGEvrfwTKDGRWRL---LEASgAPIKKNGEVDG-------- 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  676 sdnAVYICgwQDITETRDLinalEVEKNKAIKATVAkSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQ--------- 746
Cdd:COG5809  244 ---IVIIF--RDITERKKL----EELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKtyldimlse 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  747 --RVEAIslayatgqsllglIGEILDVDKIESGNYQLqpqwVDIPTLVQNTCHSFGAIAASKSIALSCSStFPEHYLVKI 824
Cdd:COG5809  314 ldRIESI-------------ISEFLVLAKPQAIKYEP----KDLNTLIEEVIPLLQPQALLKNVQIELEL-EDDIPDILG 375
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQVLSNLLSNALKFTTEGaVKITTSLGHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTsagrQQTGSGLGL 904
Cdd:COG5809  376 DENQLKQVFINLLKNAIEAMPEG-GNITIETKAEDDDKVVI--SVTDEGCGIPEERLKKLGEPFYTT----KEKGTGLGL 448
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 16130302  905 MICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQV 942
Cdd:COG5809  449 MVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQV 486
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
303-519 2.99e-39

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 145.55  E-value: 2.99e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     303 NLKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSpITVSHNIHAGTQLSPGGWDIIPGAI-YSEDRENNVLF 381
Cdd:smart00062    1 TLRVGTNGDYPPFSFADEDGELTGFDVDLAKAIAKELGLKVE-FVEVSFDSLLTALKSGKIDVVAAGMtITPERAKQVDF 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     382 AEAFITTPYVFVMQKAPD--SEQTL--KKGMKVAIPYYYELhsqLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQL 457
Cdd:smart00062   80 SDPYYRSGQVILVRKDSPikSLEDLkgKKVAVVAGTTAEEL---LKKLYPEAKIVSYDSNAEALAALKAGRADAAVADAP 156
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130302     458 nSRYMIDHYYPNELYHFLIPGVPN-ASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKWI 519
Cdd:smart00062  157 -LLAALVKQHGLPELKIVPDPLDTpEGYAIAVRKGDPELLDKINKALKELKADGTLkKISEKWF 219
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
961-1070 4.04e-37

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 135.29  E-value: 4.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQ---NSSLPIWGLT 1037
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELeggGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16130302 1038 ANAQANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
570-937 1.24e-36

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 142.29  E-value: 1.24e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  570 DLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFtaDYYKNAMLplensDSPFKDVFSNAHEVTA---ETKENR 646
Cdd:COG3852    1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLL--GLSAEELL-----GRPLAELFPEDSPLRElleRALAEG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  647 TIYTQ---VFEIDNGIEKRCINHWHTLCNLPASDNAVYICgwQDITETRDLINAL-EVEKNKAIKatvaksQFLATMSHE 722
Cdd:COG3852   74 QPVTErevTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVL--RDITERKRLERELrRAEKLAAVG------ELAAGLAHE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  723 IRTPISSIMGFLELLSGSgLSKEQRVEAISLAYATGQSLLGLIGEILDVdkieSGNYQLQPQWVDIPTLVQNTCHSFGA- 801
Cdd:COG3852  146 IRNPLTGIRGAAQLLERE-LPDDELREYTQLIIEEADRLNNLVDRLLSF----SRPRPPEREPVNLHEVLERVLELLRAe 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  802 IAASKSIALSCSSTFPEhylVKIDPQAFKQVLSNLLSNALKFTTEGA-VKITTSLGHIDDNHA-----VIKMTIMDSGSG 875
Cdd:COG3852  221 APKNIRIVRDYDPSLPE---VLGDPDQLIQVLLNLVRNAAEAMPEGGtITIRTRVERQVTLGGlrprlYVRIEVIDNGPG 297
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130302  876 LSQEEQQQLFK-RYSqtsaGRQQtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVE 937
Cdd:COG3852  298 IPEEILDRIFEpFFT----TKEK-GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
536-941 1.31e-36

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 143.95  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  536 FYIVTTLSVLLVGSSLLW-GFYLLRSVRR---------RKVIQGDLENQIS----------------------------- 576
Cdd:COG5000    7 FLLLLLLIALLLLLLALWlALLLARRLTRplrrlaeatRAVAAGDLSVRLPvtgddeigelarafnrmtdqlkeqreele 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  577 ----FRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFTADyyknamlPLENSDSPFKDVFSNAHEVTAETKENRTIYTQV 652
Cdd:COG5000   87 errrYLETILENLPAGVIVLDADGRITLANPAAERLLGIP-------LEELIGKPLEELLPELDLAELLREALERGWQEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  653 FEIDNGIEKRCinhwhtLCNLPASDNAVYICGWQDITEtrdLINAlevEKNKAIKatvaksQFLATMSHEIRTPISSIMG 732
Cdd:COG5000  160 IELTRDGRRTL------LVRASPLRDDGYVIVFDDITE---LLRA---ERLAAWG------ELARRIAHEIKNPLTPIQL 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  733 FLELL-----SGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIEsgnyQLQPQWVDIPTLVQNTCHSFGAIAASKS 807
Cdd:COG5000  222 SAERLrrklaDKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLREVLALYEPALKEKD 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  808 IALSCSSTfPEHYLVKIDPQAFKQVLSNLLSNALKFTTE-GAVKITTslgHIDDNHAVIkmTIMDSGSGLSQEEQQQLFK 886
Cdd:COG5000  298 IRLELDLD-PDLPEVLADRDQLEQVLINLLKNAIEAIEEgGEIEVST---RREDGRVRI--EVSDNGPGIPEEVLERIFE 371
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  887 RYSQTsagrQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQ 941
Cdd:COG5000  372 PFFTT----KPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEAE 422
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
524-937 1.38e-35

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 142.62  E-value: 1.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  524 VTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRSVRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNS 603
Cdd:COG4251   86 LLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLA 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  604 AFEHYFTADYYKNAMLPLENSDSPFKDVFSNAHEVTAETKENRTIYTQVFEIDNGIEKRCINHWHTLCNLPASDNAVYIC 683
Cdd:COG4251  166 LILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLL 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  684 GWQDITETRDLINALEVEKNKAIKATVAK--------SQFLATMSHEIRTPISSIMGFLELLS---GSGLSKEQRvEAIS 752
Cdd:COG4251  246 LLLILVLELLELRLELEELEEELEERTAElersneelEQFAYVASHDLREPLRKISGFSQLLEedyGDKLDEEGR-EYLE 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  753 LAYATGQSLLGLIGEILDVDKIesGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSStFPEhylVKIDPQAFKQV 832
Cdd:COG4251  325 RIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGP-LPT---VRGDPTLLRQV 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  833 LSNLLSNALKFTTEGA---VKITtslGHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKE 909
Cdd:COG4251  399 FQNLISNAIKYSRPGEpprIEIG---AEREGGEWVF--SVRDNGIGIDPEYAEKIFEIFQRLHSRDEYEGTGIGLAIVKK 473
                        410       420
                 ....*....|....*....|....*...
gi 16130302  910 LIKNMQGDLSLESHPGIGTTFTITIPVE 937
Cdd:COG4251  474 IVERHGGRIWVESEPGEGATFYFTLPKA 501
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
304-520 2.62e-34

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 131.26  E-value: 2.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  304 LKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSHN--IHAgtqLSPGGWDIIPGAI-YSEDRENNVL 380
Cdd:COG0834    1 LRVGVDPDYPPFSFRDEDGKLVGFDVDLARAIAKRLGLKVEFVPVPWDrlIPA---LQSGKVDLIIAGMtITPEREKQVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  381 FAEAFITTPYVFVMQKAPDSEQTLK--KGMKVAIP--YYYELHsqLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQ 456
Cdd:COG0834   78 FSDPYYTSGQVLLVRKDNSGIKSLAdlKGKTVGVQagTTYEEY--LKKLGPNAEIVEFDSYAEALQALASGRVDAVVTDE 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  457 LNSRYMIDHYyPNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKWIK 520
Cdd:COG0834  156 PVAAYLLAKN-PGDDLKIVGEPLSGEPYGIAVRKGDPELLEAVNKALAALKADGTLdKILEKWFG 219
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
956-1073 2.75e-34

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 127.66  E-value: 2.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  956 PEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLR--EQNSSLPI 1033
Cdd:COG0784    3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRalPRLPDIPI 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 16130302 1034 WGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
Cdd:COG0784   83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
571-934 4.36e-33

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 131.18  E-value: 4.36e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    571 LENQIS-FRKALSdSLPNPTYVVNWQGNVISHNSAFEHYFTADYYKNAMLPLEN--SDSPFKDVFSNAH-----EVTAET 642
Cdd:TIGR02966    1 LSALLSrFRAAAQ-ALPDAVVVLDEEGQIEWCNPAAERLLGLRWPDDLGQRITNliRHPEFVEYLAAGRfseplELPSPI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    643 KENRTIYTQVFeidngiekrcinhwhtlcnlPASDNAVYICgWQDITETRDLINAleveknkaikatvaKSQFLATMSHE 722
Cdd:TIGR02966   80 NSERVLEIRIA--------------------PYGEEQKLLV-ARDVTRLRRLEQM--------------RRDFVANVSHE 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    723 IRTPISSIMGFLELLSGSG-LSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGA 801
Cdd:TIGR02966  125 LRTPLTVLRGYLETLADGPdEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEA 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    802 IAASKS--IALSCSSTFPehylVKIDPQAFKQVLSNLLSNALKFTTEGAvKITTSLgHIDDNHAVIKMTimDSGSGLSQE 879
Cdd:TIGR02966  205 LSQGKNhqITFEIDGGVD----VLGDEDELRSAFSNLVSNAIKYTPEGG-TITVRW-RRDGGGAEFSVT--DTGIGIAPE 276
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302    880 EQQQLFKRYSQTSAGR--QQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI 934
Cdd:TIGR02966  277 HLPRLTERFYRVDKSRsrDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFIF 333
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
961-1070 5.18e-33

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 123.42  E-value: 5.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 16130302   1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
Cdd:pfam00072   81 DEDDAVEALEAGADDFLSKPFDPDELLAAI 110
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
714-936 2.27e-32

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 129.92  E-value: 2.27e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  714 QFLATMSHEIRTPISSIMGFLELLS---GSGLSKEQRVEAISLAYATGQSLLGLIGEILDVdkieSGNYQLQPQWVDIPT 790
Cdd:COG4191  144 ELAAGIAHEINNPLAAILGNAELLRrrlEDEPDPEELREALERILEGAERAAEIVRSLRAF----SRRDEEEREPVDLNE 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  791 LVQNTCHSFGAIAASKSIALSCSSTfPEHYLVKIDPQAFKQVLSNLLSN---ALKFTTEGAVKITTSLghiDDNHAVIkm 867
Cdd:COG4191  220 LIDEALELLRPRLKARGIEVELDLP-PDLPPVLGDPGQLEQVLLNLLINaidAMEEGEGGRITISTRR---EGDYVVI-- 293
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  868 TIMDSGSGLSQEEQQQLF------KRYSQtsagrqqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:COG4191  294 SVRDNGPGIPPEVLERIFepffttKPVGK--------GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
824-937 4.78e-32

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 120.83  E-value: 4.78e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     824 IDPQAFKQVLSNLLSNALKFTTEGaVKITTSLgHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQT-GSGL 902
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEG-GRITVTL-ERDGDHVEI--TVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIgGTGL 76
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 16130302     903 GLMICKELIKNMQGDLSLESHPGIGTTFTITIPVE 937
Cdd:smart00387   77 GLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
713-936 1.92e-31

Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 128.45  E-value: 1.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  713 SQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLqpqwVDIPTLV 792
Cdd:COG5806  202 SELAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKLEK----IDVSEEL 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  793 QNTCHSFGAIAASKSIALSCssTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTE-GAVKITTSlghIDDNHAVIkmTIMD 871
Cdd:COG5806  278 EHVIDVLSPYANMNNVEIQT--ELEPGLYIEGDRQKLQQCLINIIKNGIEAMPNgGTLTIDVS---IDKNKVII--SIKD 350
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  872 SGSGLSQEEQQQLFKRYSQTsagrQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:COG5806  351 TGVGMTKEQLERLGEPYFST----KEKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLPL 411
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
958-1070 1.38e-29

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 116.16  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  958 KLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLRE--QNSSLPIWG 1035
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAdpRTADIPIIF 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 16130302 1036 LTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
713-939 2.01e-29

Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 123.32  E-value: 2.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  713 SQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESGNYQLqpqwVDIPTLV 792
Cdd:COG5808  242 GTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQ-KYFDIIQEEIQRINQIVSEFLVLGKPTAKKLEL----DDLNELI 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  793 QNTCHSFGAIAASKSIALSCSSTfPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGAvKITTSLGHiDDNHAVIKmtIMDS 872
Cdd:COG5808  317 EEILSIIDSEANLKNIRVEKQSL-DEPLHIKCDKDRIKQVLLNLIKNAIEAMKEGG-KLTISIEN-DDEKAVIE--VIDN 391
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302  873 GSGLSQEEQQQLFKRYSQTSagrqQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEIS 939
Cdd:COG5808  392 GEGIPEDIIDEIFEPFVTTK----EGGTGLGLSVCKRIVEMHGGEIDIESEEGKGTTFTIRLPLKKE 454
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
958-1139 3.66e-29

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 115.82  E-value: 3.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  958 KLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLT 1037
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302 1038 ANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL-----HQVAHIAPQYRHLDIEALKNN-----TANDLQLMqEILM 1107
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALlrrraAEVLRVGDLLDLAAREVTRDGepvelTPKEFRLL-ELLM 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 16130302 1108 TFQHE--THKDLPAAFQALEAGDNRTFHQCIHRI 1139
Cdd:COG0745  160 RNPGRvvSREQLLEEVWGYDYGDDRTVDVHISRL 193
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
570-936 3.87e-29

Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 120.28  E-value: 3.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  570 DLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEHYFT--ADYYKNAMLPLENSDSPFKDVFsNAHEVTAETKENRT 647
Cdd:COG5807   21 LTEDSEFKFKQLFDSILEFVFFIDSKGEILECNDFAEDLYGlsQNEYIGKTFVEEKCILKDEQLY-NKEAFDRIEISYLT 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  648 IYTQVFEIDNGIEKRCINhwhtlcnlpasdNAVYICGWQDITETRDLinalEVEKNKAIKATVAKsQFLATMSHEIRTPI 727
Cdd:COG5807  100 KNGEFDEIIYPIYYKDGV------------ILGLITVYRDITKRKEA----EDKLLRSEKLSVAG-ELAAGIAHEIRNPL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  728 SSIMGFLELL--SGSGLSKEQRVEAIslaYATGQSLLGLIGEILDVDKIESGNYQLQPqwvdIPTLVQNTCHSFGAIAAS 805
Cdd:COG5807  163 TSIKGFLQLLqeSREDSEREEYFNII---ISEIDRINTIITELLVLSKPKKFNFKKLN----LNDVLEDVIALLSTEAIL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  806 KSIALSCSstFPEH-YLVKIDPQAFKQVLSNLLSNALK-FTTEGAVKITTSlghIDDNHAVIkmTIMDSGSGLSQEEQQQ 883
Cdd:COG5807  236 KNISIKYD--LADDePVINGDKNQLKQVFINLIKNAIEaMETGGNITIKTY---VEGDFVVI--SVKDEGIGIPEEVLEK 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16130302  884 LFKRYSQTsagrQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:COG5807  309 IGEPFFTT----KEEGTGLGLSICKKIIEEHNGTIEVESKPGKGTTFTIYLPL 357
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
825-938 1.99e-28

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 110.54  E-value: 1.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    825 DPQAFKQVLSNLLSNALKFTTE-GAVKITTSlghiDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAgRQQTGSGLG 903
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKaGEITVTLS----EGGELTL--TVEDNGIGIPPEDLPRIFEPFSTADK-RGGGGTGLG 74
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 16130302    904 LMICKELIKNMQGDLSLESHPGIGTTFTITIPVEI 938
Cdd:pfam02518   75 LSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
74-276 4.24e-28

The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 113.40  E-value: 4.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   74 DSQQRVRGINADYLNLLKRALNIKLTLREYADHQKAMDALAEGEVDIvLSHLVTSPPLNNDIAATKPLIITFPALVTtlH 153
Cdd:cd01007   19 DEGGEPQGIAADYLKLIAKKLGLKFEYVPGDSWSELLEALKAGEIDL-LSSVSKTPEREKYLLFTKPYLSSPLVIVT--R 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  154 DSMRPLTSPKPVNIARVA---NYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSLNV 230
Cdd:cd01007   96 KDAPFINSLSDLAGKRVAvvkGYALEELLRERYPNINLVEVDSTEEALEAVASGEADAYIGNLAVASYLIQKYGLSNLKI 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 16130302  231 VKYYNSPRQYNfFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWL 276
Cdd:cd01007  176 AGLTDYPQDLS-FAVRKDWPELLSILNKALASISPEERQAIRNKWL 220
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
591-941 4.39e-27

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 118.15  E-value: 4.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   591 VVNWQGNVISHNSAFEHyftadyyknaMLPLENSD---SPFKDVFSN----AHEVTAETKENRTIYTQVFEI---DNGIE 660
Cdd:PRK11360  277 AIDRQGKITTMNPAAEV----------ITGLQRHElvgKPYSELFPPntpfASPLLDTLEHGTEHVDLEISFpgrDRTIE 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   661 krcinhwhtlcnLPASDN-----------AVYICgwQDITETRdlinALEVEKNKAIK-ATVAKsqFLATMSHEIRTPIS 728
Cdd:PRK11360  347 ------------LSVSTSllhnthgemigALVIF--SDLTERK----RLQRRVARQERlAALGE--LVAGVAHEIRNPLT 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   729 SIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIEsgnyQLQPQWVDIPTLVQNTCHSFGAIAASKSI 808
Cdd:PRK11360  407 AIRGYVQIWRQQTSDPPSQ-EYLSVVLREVDRLNKVIDQLLEFSRPR----ESQWQPVSLNALVEEVLQLFQTAGVQARV 481
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   809 ALS--CSSTFPehyLVKIDPQAFKQVLSNLLSNALK-FTTEGAVKITTSLghIDDNHAVIkmTIMDSGSGLSQEEQQQLF 885
Cdd:PRK11360  482 DFEteLDNELP---PIWADPELLKQVLLNILINAVQaISARGKIRIRTWQ--YSDGQVAV--SIEDNGCGIDPELLKKIF 554
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302   886 KRYSQTSAgrqqTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQ 941
Cdd:PRK11360  555 DPFFTTKA----KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQGN 606
PBP2_BvgS_D1 cd13705
The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
309-519 4.48e-26

The first of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the first domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270423 [Multi-domain]  Cd Length: 221  Bit Score: 107.68  E-value: 4.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  309 NPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSpITVSHNIHAGTQ-LSPGGWDIIPGAIYSEDRENNVLFAEAFIT 387
Cdd:cd13705   10 APDYPPFDITSSGGRYEGITADYLGLIADALGVRVE-VRRYPDREAALEaLRNGEIDLLGTANGSEAGDGGLLLSQPYLP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  388 TPYVFVMQKAPDSEQTL-KKGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRYMIDHY 466
Cdd:cd13705   89 DQPVLVTRIGDSRQPPPdLAGKRVAVVPGYLPAEEIKQAYPDARIVLYPSPLQALAAVAFGQADYFLGDAISANYLISRN 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16130302  467 YPNELY-HFLIPgVPNASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWI 519
Cdd:cd13705  169 YLNNLRiVRFAP-LPSRGFGFAVRPDNTRLLRLLNRALAAIPDEQRDEILRRWS 221
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
528-936 7.37e-26

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 113.29  E-value: 7.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  528 TWDLYSEQFYIVTTLsVLLVGSSLLWGFYLLRSVRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSAFEH 607
Cdd:COG5805  110 IYCKDGELIYVEVKL-FPIYNQNGQAAILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIER 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  608 YFTADYY----KNAmlpLENSDSPFKDVFSNAHEVTAETKENRTIYTQVFEIDNGI---EKRCINHWHTLCNLPAsdnav 680
Cdd:COG5805  189 LFGAPREeligKNL---LELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIryfEAVIVPLIDTDGSVKG----- 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  681 YICGWQDITETRDLinalEVEKNKAIKATVAkSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQ----------RVEA 750
Cdd:COG5805  261 ILVILRDITEKKEA----EELMARSEKLSIA-GQLAAGIAHEIRNPLTSIKGFLQLLQPGIEDKEEyfdimlseldRIES 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  751 IslayatgqsllglIGEILDVDKIESGNYQLqpqwVDIPTLVQNTCHSFG--AIAASKSIALSCSSTFPEhylVKIDPQA 828
Cdd:COG5805  336 I-------------ISEFLALAKPQAVNKEK----ENINELIQDVVTLLEteAILHNIQIRLELLDEDPF---IYCDENQ 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  829 FKQVLSNLLSNALK-FTTEGAVKIttslgHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTsagrQQTGSGLGLMIC 907
Cdd:COG5805  396 IKQVFINLIKNAIEaMPNGGTITI-----HTEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTT----KEKGTGLGLMVS 466
                        410       420
                 ....*....|....*....|....*....
gi 16130302  908 KELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:COG5805  467 YKIIENHNGTIDIDSKVGKGTTFTITLPL 495
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
304-519 1.21e-25

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 106.22  E-value: 1.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    304 LKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLN--FSPITVSHNIhagTQLSPGGWDIIPGAIY-SEDRENNVL 380
Cdd:pfam00497    1 LRVGTDGDYPPFEYVDENGKLVGFDVDLAKAIAKRLGVKveFVPVSWDGLI---PALQSGKVDLIIAGMTiTPERAKQVD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    381 FAEAFITTPYVFVMQKApDSEQTLK-----KGMKVAIP---YYYELHSQLKEmyPEVEWIQVDNASAAFHKVKEGELDAL 452
Cdd:pfam00497   78 FSDPYYYSGQVILVRKK-DSSKSIKsladlKGKTVGVQkgsTAEELLKNLKL--PGAEIVEYDDDAEALQALANGRVDAV 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130302    453 VATQLNSRYMIDHYyPNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKWI 519
Cdd:pfam00497  155 VADSPVAAYLIKKN-PGLNLVVVGEPLSPEPYGIAVRKGDPELLAAVNKALAELKADGTLaKIYEKWF 221
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
956-1091 5.98e-24

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 101.40  E-value: 5.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  956 PEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSS--LPI 1033
Cdd:COG3437    4 GQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTrdIPV 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130302 1034 WGLTANAQANEREKGLSCGMNLCLFKPLTLDVL----KTHLSQLHQVAHIAPQYRHLDIEAL 1091
Cdd:COG3437   84 IFLTALADPEDRERALEAGADDYLTKPFDPEELlarvRNALELRRLQRELDDLVLYLKLAAP 145
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
960-1066 7.94e-24

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 97.76  E-value: 7.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNS--SLPIWGLT 1037
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAykFTPILMLT 81
                         90       100
                 ....*....|....*....|....*....
gi 16130302 1038 ANAQANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd17562   82 TESSDEKKQEGKAAGATGWLVKPFDPEQL 110
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
962-1052 4.84e-23

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 94.78  E-value: 4.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  962 LIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQ 1041
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                         90
                 ....*....|.
gi 16130302 1042 ANEREKGLSCG 1052
Cdd:cd17574   81 EEDKVLGLELG 91
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
962-1060 1.24e-22

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 93.45  E-value: 1.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  962 LIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQ 1041
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 16130302 1042 ANEREKGLSCGMNLCLFKP 1060
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
701-941 1.48e-22

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 102.40  E-value: 1.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   701 EKNKAIKatvakSQFLATMSHEIRTPISSIMGFLELLSgSGLSKeqrveaislayATGQSLLGLIGEILDVDKIESGNYQ 780
Cdd:PRK10549  234 EKNEQMR-----RDFMADISHELRTPLAVLRGELEAIQ-DGVRK-----------FTPESVASLQAEVGTLTKLVDDLHQ 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   781 L----------QPQWVDIPTLVQNTCHSFGAIAASKSIALSCSstFPEHYLVKIDPQAFKQVLSNLLSNALKFTTE-GAV 849
Cdd:PRK10549  297 LslsdegalayRKTPVDLVPLLEVAGGAFRERFASRGLTLQLS--LPDSATVFGDPDRLMQLFNNLLENSLRYTDSgGSL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   850 KITtslGHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRY--SQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIG 927
Cdd:PRK10549  375 HIS---AEQRDKTLRL--TFADSAPGVSDEQLQKLFERFyrTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGG 449
                         250
                  ....*....|....
gi 16130302   928 TTFTITIPVEISQQ 941
Cdd:PRK10549  450 VSITVELPLERDLQ 463
PBP2_BvgS_like_1 cd13708
Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is ...
313-519 2.34e-22

Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270426 [Multi-domain]  Cd Length: 220  Bit Score: 96.81  E-value: 2.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  313 PPYSMTDENGSVRGVMGDILNIITLQTGLNFSPI-TVS--HNIHAGTQlspGGWDIIPGAIYSEDRENNVLFAEAFITTP 389
Cdd:cd13708   13 MPYEGIDEGGKHVGIAADYLKLIAERLGIPIELVpTKSwsESLEAAKE---GKCDILSLLNQTPEREEYLNFTKPYLSDP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  390 YVFVMQKAPDSEQTLK--KGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRYMIDHYY 467
Cdd:cd13708   90 NVLVTREDHPFIADLSdlGDKTIGVVKGYAIEEILRQKYPNLNIVEVDSEEEGLKKVSNGELFGFIDSLPVAAYTIQKEG 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16130302  468 PNELYhflIPGVPNA--SLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWI 519
Cdd:cd13708  170 LFNLK---ISGKLDEdnELRIGVRKDEPLLLSILNKAIASITPEERQEILNKWV 220
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
959-1073 3.13e-22

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 93.17  E-value: 3.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  959 LSILIADDHPTNRLLLKRQLNLLGY-DVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLR--EQNSSLPIWG 1035
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGFnNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRadGALSHLPVLM 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16130302 1036 LTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
Cdd:cd19923   81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKI 118
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
961-1066 1.54e-21

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 90.98  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQ--NSSLPIWGLTA 1038
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELpwLANTPAIALTG 80
                         90       100
                 ....*....|....*....|....*...
gi 16130302 1039 NAQANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDEL 108
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
712-935 3.00e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 98.36  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   712 KSQFLATMSHEIRTPISSIMGFLELLSgSGLSKEQRVEAISLAYATGQsLLGLIGEILDVDKIESGN--YQLQPqwVDIP 789
Cdd:NF012163  240 RRDFMADISHELRTPLAVLRAELEAIQ-DGIRKFTPESLDSLQAEVGT-LTKLVDDLHDLSMSDEGAlaYQKAS--VDLV 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   790 TLVQNTCHSFGAIAASKSIALSCSstFPEHYLVKIDPQAFKQVLSNLLSNALKFT-TEGAVKITTSlghidDNHAVIKMT 868
Cdd:NF012163  316 PLLEVEGGAFRERFASAGLELEVS--LPDSSLVFGDRDRLMQLFNNLLENSLRYTdSGGSLHISAS-----QRPKEVTLT 388
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130302   869 IMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:NF012163  389 VADSAPGVSDEQLARLFERFYRVevSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
961-1061 3.19e-21

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 89.91  E-value: 3.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPIWGLTA 1038
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPatRDIPVIALTA 81
                         90       100
                 ....*....|....*....|...
gi 16130302 1039 NAQANEREKGLSCGMNLCLFKPL 1061
Cdd:cd17548   82 YAMKGDREKILEAGCDGYISKPI 104
PRK10490 PRK10490
sensor protein KdpD; Provisional
716-937 4.39e-21

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 100.11  E-value: 4.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   716 LATMSHEIRTPISSIMGFLELLSGSgLSKEQRVEAISlAYATGQSLLG---LIGEILDVDKIESGNYQLQPQWVDIPTLV 792
Cdd:PRK10490  668 LAALSHDLRTPLTVLFGQAEILTLD-LASEGSPHARQ-ASEIRQQVLNttrLVNNLLDMARIQSGGFNLRKEWLTLEEVV 745
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   793 QNTCHSFGAIAASKSIALSCSSTFPehyLVKIDPQAFKQVLSNLLSNALKFTTEGAvKITTSlGHIDDNHavIKMTIMDS 872
Cdd:PRK10490  746 GSALQMLEPGLSGHPINLSLPEPLT---LIHVDGPLFERVLINLLENAVKYAGAQA-EIGID-AHVEGER--LQLDVWDN 818
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130302   873 GSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVE 937
Cdd:PRK10490  819 GPGIPPGQEQLIFDKFARGNKESAIPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLE 883
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
690-936 7.66e-21

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 97.22  E-value: 7.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   690 ETRDLINALEVEKNK-AIKATVAksQFLATMSHEIRTPISSIMGFLELLSGSgLSKEQRVEAISLAYATGQSLLGLIGEI 768
Cdd:PRK11100  235 ELRELAQALESMRVKlEGKAYVE--QYVQTLTHELKSPLAAIRGAAELLQED-PPPEDRARFTGNILTQSARLQQLIDRL 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   769 LDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSstfPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGA 848
Cdd:PRK11100  312 LELARLEQRQELEVLEPVALAALLEELVEAREAQAAAKGITLRLR---PDDARVLGDPFLLRQALGNLLDNAIDFSPEGG 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   849 VkITTSLGHIDDNHAVikmTIMDSGSGLSQEEQQQLFKR-YSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIG 927
Cdd:PRK11100  389 T-ITLSAEVDGEQVAL---SVEDQGPGIPDYALPRIFERfYSLPRPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGG 464

                  ....*....
gi 16130302   928 TTFTITIPV 936
Cdd:PRK11100  465 VLATLTLPR 473
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
309-518 9.47e-21

The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 92.26  E-value: 9.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  309 NPYSPPYSMTDENGSVRGVMGDILNIITLQTGLN--FSPITVSHNIhagTQLSPGGWDIIPGAIYSEDRENNVLFAEAFI 386
Cdd:cd13704    9 DKNYPPYEFLDENGNPTGFNVDLLRAIAEEMGLKveIRLGPWSEVL---QALENGEIDVLIGMAYSEERAKLFDFSDPYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  387 TTPYVFVMQKAPDSEQTLK--KGMKVAI---PYYYELhsqLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRY 461
Cdd:cd13704   86 EVSVSIFVRKGSSIINSLEdlKGKKVAVqrgDIMHEY---LKERGLGINLVLVDSPEEALRLLASGKVDAAVVDRLVGLY 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130302  462 MIDHYYPNELyHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKW 518
Cdd:cd13704  163 LIKELGLTNV-KIVGPPLLPLKYCFAVRKGNPELLAKLNEGLAILKASGEYdEIYEKW 219
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
713-935 2.58e-20

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 95.53  E-value: 2.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    713 SQFLATMSHEIRTPISSIMGFLELLsgsgLSKEQRVEAISLAYATG----QSLLGLIGEILDVDKIESGNYQLQPQWVDI 788
Cdd:TIGR01386  242 SQFSADLAHELRTPLTNLLGQTQVA----LSQPRTGEEYREVLESNleelERLSRMVSDMLFLARADNGQLALERVRLDL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    789 PTLVQNTCHSFGAIA--ASKSIALSCSSTfpehylVKIDPQAFKQVLSNLLSNALKFTTEGAvKITTSLGHiDDNHAVIK 866
Cdd:TIGR01386  318 AAELAKVAEYFEPLAeeRGVRIRVEGEGL------VRGDPQMFRRAISNLLSNALRHTPDGG-TITVRIER-RSDEVRVS 389
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302    867 MTimDSGSGLSQEEQQQLFKRYSQTSAGRQ--QTGSGLGLMICKELIKNMQGDLSLESHPGiGTTFTITIP 935
Cdd:TIGR01386  390 VS--NPGPGIPPEHLSRLFDRFYRVDPARSnsGEGTGLGLAIVRSIMEAHGGRASAESPDG-KTRFILRFP 457
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
961-1066 3.56e-20

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 87.05  E-value: 3.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                         90       100
                 ....*....|....*....|....*.
gi 16130302 1041 QANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd17627   81 SVSDRVAGLDAGADDYLVKPFALEEL 106
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
710-941 4.62e-20

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 94.85  E-value: 4.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   710 VAKSQFLATMSHEIRTPISSIMGFLELLSgsglskeQRVEAISLAYATGQSLLG-------LIGEILDVDKIEsgnyQLQ 782
Cdd:PRK10364  235 VALGHLAAGVAHEIRNPLSSIKGLAKYFA-------ERAPAGGEAHQLAQVMAKeadrlnrVVSELLELVKPT----HLA 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   783 PQWVDIPTLVQntcHSFGAI---AASKSIALSCSSTfPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVkITTSLGHID 859
Cdd:PRK10364  304 LQAVDLNDLIN---HSLQLVsqdANSREIQLRFTAN-DTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGV-ISVTASESG 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   860 DNhavIKMTIMDSGSGLSQEEQQQLFKRYSQTSAgrqqTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEIS 939
Cdd:PRK10364  379 AG---VKISVTDSGKGIAADQLEAIFTPYFTTKA----EGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNIT 451

                  ..
gi 16130302   940 QQ 941
Cdd:PRK10364  452 RR 453
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
957-1073 7.03e-20

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 93.87  E-value: 7.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  957 EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGL 1036
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16130302 1037 TANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERA 117
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
1098-1190 5.07e-19

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 83.07  E-value: 5.07e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    1098 DLQLMQEILMTFQHETHKDLPAAFQALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEITPVSDDSKPEilQLLNS 1177
Cdd:smart00073    2 GLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEV--ELTPD 79
                            90
                    ....*....|...
gi 16130302    1178 VKEHIAELDQEIA 1190
Cdd:smart00073   80 LLDLLLELVDVLK 92
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
960-1060 5.52e-19

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 83.28  E-value: 5.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  960 SILIADDHPTNRLLLKRQ-LNLLGYD-VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLT 1037
Cdd:COG4753    1 KVLIVDDEPLIREGLKRIlEWEAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                         90       100
                 ....*....|....*....|...
gi 16130302 1038 ANAQANEREKGLSCGMNLCLFKP 1060
Cdd:COG4753   81 GYSDFEYAQEAIKLGADDYLLKP 103
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
962-1066 1.15e-18

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 82.65  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  962 LIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQ 1041
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90       100
                 ....*....|....*....|....*
gi 16130302 1042 ANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAEL 105
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
825-935 1.20e-18

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 82.51  E-value: 1.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQVLSNLLSNALKFTTEGAvKITTSLGHIDDnhaVIKMTIMDSGSGLSQEEQQQLFKRY--SQTSAGRQQTGSGL 902
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRAAQTPQ---EVRLDVEDSAPGVSDDQLARLFERFyrVESSRNRASGGSGL 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16130302  903 GLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16946   77 GLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
PRK09303 PRK09303
histidine kinase;
698-936 2.81e-18

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 88.47  E-value: 2.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   698 LEVEKNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELL------SGSGLSKEQRVEAISLAYATGQSLLGLIGEILDV 771
Cdd:PRK09303  137 LRQENETLLEQLKFKDRVLAMLAHDLRTPLTAASLALETLelgqidEDTELKPALIEQLQDQARRQLEEIERLITDLLEV 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   772 DKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCS--STFPehyLVKIDPQAFKQVLSNLLSNALKFTTEGAv 849
Cdd:PRK09303  217 GRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDipSDLP---SVYADQERIRQVLLNLLDNAIKYTPEGG- 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   850 KITTSLGHIDDNHavIKMTIMDSGSGLSQEEQQQLFK---RYSQTSagrQQTGSGLGLMICKELIKNMQGDLSLESHPGI 926
Cdd:PRK09303  293 TITLSMLHRTTQK--VQVSICDTGPGIPEEEQERIFEdrvRLPRDE---GTEGYGIGLSVCRRIVRVHYGQIWVDSEPGQ 367
                         250
                  ....*....|
gi 16130302   927 GTTFTITIPV 936
Cdd:PRK09303  368 GSCFHFTLPV 377
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
711-935 3.22e-18

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 88.91  E-value: 3.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   711 AKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQPQWVDIPT 790
Cdd:PRK11006  203 ARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMREQTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPM 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   791 LVQntchsfgaIAASKSIALSCSstfpEHYLV-KIDPQ--------AFKQVLSNLLSNALKFTTEGAvKITTSLGHIdDN 861
Cdd:PRK11006  283 MLR--------VLEREAQTLSQG----KHTITfEVDNSlkvfgnedQLRSAISNLVYNAVNHTPEGT-HITVRWQRV-PQ 348
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302   862 HAVIKMTimDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:PRK11006  349 GAEFSVE--DNGPGIAPEHIPRLTERFYRVdkARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLP 422
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
825-935 3.76e-18

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 81.00  E-value: 3.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQVLSNLLSNALKFTTEGAvKITTSLGHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGL 902
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGG-RIRCILEKFRLNRFLL--TVSDSGPGIPPNLREEIFERFRQGdgSSTRAHGGTGL 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16130302  903 GLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16925   78 GLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
961-1060 3.88e-18

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 81.00  E-value: 3.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSS--LPIWGLTA 1038
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETrhIPVIMITA 81
                         90       100
                 ....*....|....*....|..
gi 16130302 1039 NAQANEREKGLSCGMNLCLFKP 1060
Cdd:cd17538   82 LDDREDRIRGLEAGADDFLSKP 103
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
686-1196 5.51e-18

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 90.10  E-value: 5.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  686 QDITETRDLINALEVEKNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLI 765
Cdd:COG2198  353 LLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLLLLLLLLLLL 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  766 GEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPEHYLVKIDPQAFKQVLSNLLSNALKFTT 845
Cdd:COG2198  433 LLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVAAALA 512
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  846 EGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLF--KRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESH 923
Cdd:COG2198  513 ALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAalLLLLALLLGLGLLLGLLLGGLLLLLLLLLLLLLLLLLL 592
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  924 PGIGTTFTITIPVEISQQVATVEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHY 1003
Cdd:COG2198  593 LLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAAALAALDLLL 672
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302 1004 DLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLC--------LFKPLTLDVLKTHLSQLHQ 1075
Cdd:COG2198  673 DLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAAllllllllLLLLLLLLLLLLAAAAAAA 752
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302 1076 VAHIAPQYRHLDIEALKNnTANDLQLMQEILMTFQHETHKDLPAAFQALEAGDNRTFHQCIHRIHGAANILNLQKLINIS 1155
Cdd:COG2198  753 ASPAAPALPVLDLEALRR-LGGDPELLRELLELFLEELPELLAELRQALAAGDLEALARLAHKLKGSAGNLGAPRLAELA 831
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 16130302 1156 HQLEiTPVSDDSKPEILQLLNSVKEHIAELDQEIAVFCQKN 1196
Cdd:COG2198  832 AELE-QAARAGDLEEAEELLAELEAELERVLAALEALLAEE 871
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
961-1060 6.60e-18

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 80.50  E-value: 6.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSM---------QHYDLLITDVNMPNMDGFELTRKLREQN--S 1029
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELRDDPrlA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 16130302 1030 SLPIWGLTANAQANEREKGLSCGMNLCLFKP 1060
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
961-1060 7.55e-18

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 79.79  E-value: 7.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                         90       100
                 ....*....|....*....|
gi 16130302 1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:cd19935   81 SVEDRVKGLDLGADDYLVKP 100
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
817-934 1.03e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 80.25  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  817 PEHYL-VKIDPQAFKQVLSNLLSNALKFTTEGAVkittsLG-HIDDNHAVIKMTIMDSGSGLSQEEQQQLFKR-YS-QTS 892
Cdd:cd16947    8 PDRPIyANANTEALQRILKNLISNAIKYGSDGKF-----LGmTLREDEKHVYIDIWDKGKGISETEKDHVFERlYTlEDS 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 16130302  893 AGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI 934
Cdd:cd16947   83 RNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
961-1052 1.24e-17

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 79.48  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLR--EQNSSLPIWGLTA 1038
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKadPATRHIPVIFLTA 80
                         90
                 ....*....|....
gi 16130302 1039 NAQANEREKGLSCG 1052
Cdd:cd19920   81 LTDTEDKVKGFELG 94
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
961-1066 2.32e-17

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 79.07  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                         90       100
                 ....*....|....*....|....*.
gi 16130302 1041 QANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd17624   81 GVDDRVAGLDAGADDYLVKPFALEEL 106
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
524-937 2.47e-17

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 85.67  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  524 VTIDTWDLYSEQFYIVTTLSVLLVGSSLLWGFYLLRSVRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNS 603
Cdd:COG3290   32 ILLLVLLLLLFLLFVIILLLLLLILLLILLLLLLLLLAALLLKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLIND 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  604 AFEhyftadyyknAMLPLENSDSPFKDVFsnaHEVTAETKENRTIYtqvfeidngiekrcINHWHTLCN-LPASDNAVYI 682
Cdd:COG3290  112 AAR----------RLLGLDAIGRPIDEVL---AEVLETGERDEEIL--------------LNGRVLVVNrVPIRDDGRVV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  683 cGW----QDITETRDLINALEVEKNKAikatvaksQFLATMSHEIRTPISSIMGFLELlsgsglskeQRVEAIsLAYAtg 758
Cdd:COG3290  165 -GAvatfRDRTELERLEEELEGVKELA--------EALRAQRHDFRNHLHTISGLLQL---------GEYDEA-LEYI-- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  759 QSLLGLIGEILDVDKIESGNYqlqpqwvdiptLVQNTCHSFGAIAASKSIALS--CSSTFPEhylVKIDPQAFKQVLSNL 836
Cdd:COG3290  224 DEISEELQELIDSLLSRIGNP-----------VLAALLLGKAARARERGIDLTidIDSDLPD---LPLSDTDLVTILGNL 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  837 LSNALkfttEGAVKITTSLGHI------DDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRqqtGSGLGLMICKEL 910
Cdd:COG3290  290 LDNAI----EAVEKLPEEERRVelsirdDGDELVI--EVEDSGPGIPEELLEKIFERGFSTKLGE---GRGLGLALVKQI 360
                        410       420
                 ....*....|....*....|....*..
gi 16130302  911 IKNMQGDLSLESHPGIGTTFTITIPVE 937
Cdd:COG3290  361 VEKYGGTIEVESEEGEGTVFTVRLPKE 387
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
961-1073 2.81e-17

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 79.07  E-value: 2.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:COG5803    5 ILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTAYG 84
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16130302 1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
Cdd:COG5803   85 ELDMVEEAKELGAKGYFTKPFDIDELREAVNKL 117
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
73-278 4.99e-17

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 81.56  E-value: 4.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   73 TDSQQRVRGINADYLNLLKRALNIKLTLREYaDHQKAMDALAEGEVDIVLSHLVTSPPLNNDIAATKPLIITFPALVTtl 152
Cdd:COG0834   15 RDEDGKLVGFDVDLARAIAKRLGLKVEFVPV-PWDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPYYTSGQVLLV-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  153 HDSMRPLTSP---KPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSLN 229
Cdd:COG0834   92 RKDNSGIKSLadlKGKTVGVQAGTTYEEYLKKLGPNAEIVEFDSYAEALQALASGRVDAVVTDEPVAAYLLAKNPGDDLK 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16130302  230 VVKYYNSPRQYnFFLTRKESVILNEVLNRFVDALTNEVRY-EVSQNWLDT 278
Cdd:COG0834  172 IVGEPLSGEPY-GIAVRKGDPELLEAVNKALAALKADGTLdKILEKWFGE 220
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
699-1009 5.93e-17

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 86.52  E-value: 5.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   699 EVEKNkaikaTVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATgQSLLGLIGEILDVDKIESGN 778
Cdd:PRK10618  442 EYEKN-----QQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQS-DVLVRLVDNIQLLNMLETQD 515
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   779 YQLQPQWVDIPTLVQNTC-HSFGAIAAsKSIALSCSSTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGavKITTSLGH 857
Cdd:PRK10618  516 WKPEQELFSLQDLIDEVLpEVLPAIKR-KGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYG--KITLEVDQ 592
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   858 IDDNHAVIKMTIMDSGSGLSQEEQQQL-FKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:PRK10618  593 DESSPDRLTIRILDTGAGVSIKELDNLhFPFLNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKM 672
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302   937 EISQQvatvEAKAEQPITLpEKLSILIADDHPTNRLLLKRQLNLLG---YDVDEATDGvqalhkvsmQHYDLLITD 1009
Cdd:PRK10618  673 LAADP----EVEEEEEKLL-DGVTVLLDITSEEVRKIVTRQLENWGatcITPDERLIS---------QEYDIFLTD 734
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
961-1060 6.16e-17

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 77.42  E-value: 6.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPIWGLTA 1038
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNAdfDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 16130302 1039 NAQANEREKGLSCGMNLCLFKP 1060
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
711-777 6.30e-17

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 76.10  E-value: 6.30e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302    711 AKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESG 777
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQR-EYLETILRSAERLLRLINDLLDLSRIEAG 66
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
712-935 6.73e-17

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 85.21  E-value: 6.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   712 KSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVdkIESGNYQLQPQWV--DIP 789
Cdd:PRK09835  262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFL--AQADNNQLIPEKKmlDLA 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   790 TLVQNTCHSFGAIAASKSIALSCSSTfpeHYLVKIDPQAFKQVLSNLLSNALKFTTEGAvKITTSLGHIDDNhavIKMTI 869
Cdd:PRK09835  340 DEVGKVFDFFEAWAEERGVELRFVGD---PCQVAGDPLMLRRAISNLLSNALRYTPAGE-AITVRCQEVDHQ---VQLVV 412
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130302   870 MDSGSGLSQEEQQQLFKRYSQTSAGRQQT--GSGLGLMICKELIKNMQGDLSLESHPgIGTTFTITIP 935
Cdd:PRK09835  413 ENPGTPIAPEHLPRLFDRFYRVDPSRQRKgeGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLP 479
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
960-1038 7.95e-17

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 77.26  E-value: 7.95e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTA 1038
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
PBP2_HisK_like_1 cd13706
Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This ...
312-519 9.75e-17

Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This group includes periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270424 [Multi-domain]  Cd Length: 219  Bit Score: 80.30  E-value: 9.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  312 SPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVSHNiHAGTQLSPGGWDIIPGAIYSEDRENNVLFAEAFITTP-Y 390
Cdd:cd13706   12 YPPFSFLDEDGEPQGILVDLWRLWSEKTGIPVEFVLLDWN-ESLEAVRQGEADVHDGLFKSPEREKYLDFSQPIATIDtY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  391 VFVMQKAP--DSEQTLKkGMKVAIP---YYYELhsqLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRYMIDH 465
Cdd:cd13706   91 LYFHKDLSgiTNLSDLK-GFRVGVVkgdAEEEF---LRAHGPILSLVYYDNYEAMIEAAKAGEIDVFVADEPVANYYLYK 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  466 YypNELYHFLI-PGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVLRLTEKWI 519
Cdd:cd13706  167 Y--GLPDEFRPaFRLYSGQLHPAVAKGNSALLDLINRGFALISPEELARIERKWL 219
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
961-1060 1.23e-16

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 77.17  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALhKVSMQHYD--LLITDVNMPNMDGFELTRKLREQNSS--LPIWGL 1036
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEAL-EVLEQHPDikLVITDYNMPEMDGFELVREIRKKYSRdqLAIIGI 81
                         90       100
                 ....*....|....*....|....
gi 16130302 1037 TANAQANEREKGLSCGMNLCLFKP 1060
Cdd:cd17544   82 SASGDNALSARFIKAGANDFLTKP 105
PRK10604 PRK10604
sensor protein RstB; Provisional
706-936 1.24e-16

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 83.88  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   706 IKATVA-KSQFLATMSHEIRTPISSIMGFLELLSGsgLSKEqrvEAISLAYATGQsLLGLIGEILDVDKIESGNYQLQPQ 784
Cdd:PRK10604  205 INALIAsKKQLIDGIAHELRTPLVRLRYRLEMSDN--LSAA---ESQALNRDIGQ-LEALIEELLTYARLDRPQNELHLS 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   785 WVDIPTLVQNTCHSFGAIAASKSIALSCSSTfpEHYLVkIDPQAFKQVLSNLLSNALKFTtEGAVKITTSLghiDDNHAV 864
Cdd:PRK10604  279 EPDLPAWLSTHLADIQAVTPEKTVRLDTPHQ--GDYGA-LDMRLMERVLDNLLNNALRYA-HSRVRVSLLL---DGNQAC 351
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130302   865 IkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQT--GSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:PRK10604  352 L--IVEDDGPGIPPEERERVFEPFVRLDPSRDRAtgGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPV 423
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
304-518 1.31e-16

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 79.99  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  304 LKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTG--LNFSPITVSHNIHAGTQlspGGWDIIPGAIY-SEDRENNVL 380
Cdd:cd13530    2 LRVGTDADYPPFEYIDKNGKLVGFDVDLANAIAKRLGvkVEFVDTDFDGLIPALQS---GKIDVAISGMTiTPERAKVVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  381 FAEAFITTPYVFVMQKapDSEQTLK----KGMKVAIP---YYYELhsqLKEMYPEVEWIQVDNASAAFHKVKEGELDALV 453
Cdd:cd13530   79 FSDPYYYTGQVLVVKK--DSKITKTvadlKGKKVGVQagtTGEDY---AKKNLPNAEVVTYDNYPEALQALKAGRIDAVI 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302  454 ATQLNSRYMIDHYYPNelYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKW 518
Cdd:cd13530  154 TDAPVAKYYVKKNGPD--LKVVGEPLTPEPYGIAVRKGNPELLDAINKALAELKADGTLdKLLEKW 217
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
960-1063 1.80e-16

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 76.27  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTAN 1039
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ-SEVGIILVTGR 80
                         90       100
                 ....*....|....*....|....
gi 16130302 1040 AQANEREKGLSCGMNLCLFKPLTL 1063
Cdd:cd17619   81 DDEVDRIVGLEIGADDYVTKPFNP 104
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
961-1061 3.91e-16

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 75.56  E-value: 3.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGY-DVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSS--LPIWGLT 1037
Cdd:cd17551    3 ILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLedVPIVMIT 82
                         90       100
                 ....*....|....*....|....
gi 16130302 1038 ANAQANEREKGLSCGMNLCLFKPL 1061
Cdd:cd17551   83 ADTDREVRLRALEAGATDFLTKPF 106
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
74-276 4.22e-16

The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270425 [Multi-domain]  Cd Length: 221  Bit Score: 78.80  E-value: 4.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   74 DSQQRVRGINADYLNLLKRALNIKLTLREYADHQKAMDALAEGEVDIVLShLVTSPPLNNDIAATKPLIITFPALVTtlH 153
Cdd:cd13707   19 DSNGQFRGISADLLELISLRTGLRFEVVRASSPAEMIEALRSGEADMIAA-LTPSPEREDFLLFTRPYLTSPFVLVT--R 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  154 DSMRPLTSPKPVNIARVA---NYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSLNV 230
Cdd:cd13707   96 KDAAAPSSLEDLAGKRVAipaGSALEDLLRRRYPQIELVEVDNTAEALALVASGKADATVASLISARYLINHYFRDRLKI 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 16130302  231 VKYYNSPRQYNFFLTRKESVILNEVLNRFVDALT-NEVRyEVSQNWL 276
Cdd:cd13707  176 AGILGEPPAPIAFAVRRDQPELLSILDKALLSIPpDELL-ELRNRWR 221
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
711-777 6.42e-16

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 73.37  E-value: 6.42e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302     711 AKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESG 777
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQR-EYLETILREAERLLRLINDLLDLSRIEAG 66
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
961-1060 1.11e-15

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 74.24  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90       100
                 ....*....|....*....|
gi 16130302 1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKP 100
PRK15479 PRK15479
transcriptional regulator TctD;
961-1073 1.32e-15

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 77.07  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTARS 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 16130302  1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
Cdd:PRK15479   83 AVADRVKGLNVGADDYLPKPFELEELDARLRAL 115
PBP2_BvgS_like_1 cd13708
Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is ...
74-276 2.29e-15

Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270426 [Multi-domain]  Cd Length: 220  Bit Score: 76.40  E-value: 2.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   74 DSQQRVRGINADYLNLLKRALNIKLTLREYADHQKAMDALAEGEVDIvLSHLVTSPPLNNDIAATKPLIITFPALVTTL- 152
Cdd:cd13708   19 DEGGKHVGIAADYLKLIAERLGIPIELVPTKSWSESLEAAKEGKCDI-LSLLNQTPEREEYLNFTKPYLSDPNVLVTREd 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  153 HDSMRPLTSPKPVNIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSLNV-- 230
Cdd:cd13708   98 HPFIADLSDLGDKTIGVVKGYAIEEILRQKYPNLNIVEVDSEEEGLKKVSNGELFGFIDSLPVAAYTIQKEGLFNLKIsg 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 16130302  231 -VKYYNSPRqynfFLTRKESVILNEVLNRFVDALTNEVRYEVSQNWL 276
Cdd:cd13708  178 kLDEDNELR----IGVRKDEPLLLSILNKAIASITPEERQEILNKWV 220
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
961-1066 3.15e-15

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 73.16  E-value: 3.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKD 81
                         90       100
                 ....*....|....*....|....*.
gi 16130302 1041 QANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd17615   82 SVEDRIAGLTAGGDDYVTKPFSLEEV 107
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
956-1088 3.60e-15

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 73.47  E-value: 3.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  956 PEKLSILIADDHPTNRLLLKRQ-LNLLGYD-VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPI 1033
Cdd:COG4565    1 MKMIRVLIVEDDPMVAELLRRYlERLPGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDV 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16130302 1034 WGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHLDI 1088
Cdd:COG4565   81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQEEDL 135
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
959-1070 5.42e-15

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 72.43  E-value: 5.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  959 LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSM--QHYDLLITDVNMPNMDGFELT---RKLREQNSSLPI 1033
Cdd:cd19933    1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaeHSFQLVLLDLCMPEMDGFEVAlriRKLFGRRERPLI 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16130302 1034 WGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
Cdd:cd19933   81 VALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PRK10610 PRK10610
chemotaxis protein CheY;
957-1075 8.40e-15

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 72.31  E-value: 8.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   957 EKLSILIADDHPTNRLLLKRQLNLLGY-DVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPI 1033
Cdd:PRK10610    4 KELKFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALPV 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 16130302  1034 WGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQ 1075
Cdd:PRK10610   84 LMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
961-1067 1.18e-14

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 71.12  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVS--MQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTA 1038
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIRLE-MDLPVIMMSA 79
                         90       100
                 ....*....|....*....|....*....
gi 16130302 1039 NAQANEREKGLSCGMNLCLFKPLTLDVLK 1067
Cdd:cd17584   80 DGSTSTVMKGLAHGACDYLLKPVSIEDLK 108
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
961-1038 1.49e-14

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 71.00  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRL-LLKRQLNLLGYD-VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTA 1038
Cdd:cd17535    1 VLIVDDHPLVREgLRRLLESEPDIEvVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
961-1073 2.03e-14

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 70.82  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNS--SLPIWGLTA 1038
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDlkDIPVILLTT 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 16130302 1039 NAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYI 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
961-1033 4.37e-14

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 69.67  E-value: 4.37e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYD---VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPI 1033
Cdd:cd17536    1 VLIVDDEPLIREGLKKLIDWEELGfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKI 76
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
711-771 9.20e-14

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 66.85  E-value: 9.20e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302  711 AKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDV 771
Cdd:cd00082    3 AKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDL 63
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
826-936 1.04e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 68.22  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  826 PQAFKQVLSNLLSNALK-FTTEGAVKITTSlghidDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQqtGSGLGL 904
Cdd:cd16943    1 PSQLNQVLLNLLVNAAQaMEGRGRITIRTW-----AHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGE--GTGLGL 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 16130302  905 MICKELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:cd16943   74 SLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
313-518 1.50e-13

Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein fold; Cystine-binding domain of periplasmic receptor-dependent ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Also, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270344 [Multi-domain]  Cd Length: 219  Bit Score: 71.19  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  313 PPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVS-HNIHAGtqLSPGGWDIIPGAI-YSEDRENNVLFAEAFITTPY 390
Cdd:cd13626   11 PPFTFKDEDGKLTGFDVEVGREIAKRLGLKVEFKATEwDGLLPG--LNSGKFDVIANQVtITPEREEKYLFSDPYLVSGA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  391 VFVMQKAPDSEQTLK--KGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALvatqLNSRYMIDHYYP 468
Cdd:cd13626   89 QIIVKKDNTIIKSLEdlKGKVVGVSLGSNYEEVARDLANGAEVKAYGGANDALQDLANGRADAT----LNDRLAALYALK 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16130302  469 NELYHFLIPGVP--NASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKW 518
Cdd:cd13626  165 NSNLPLKIVGDIvsTAKVGFAFRKDNPELRKKVNKALAEMKADGTLkKLSEKW 217
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
73-276 1.50e-13

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 71.21  E-value: 1.50e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302      73 TDSQQRVRGINADYLNLLKRALNIKLTLREY-ADHqkAMDALAEGEVDIVLSHLVTSPPLNNDIAATKPLIITFPALVtT 151
Cdd:smart00062   16 ADEDGELTGFDVDLAKAIAKELGLKVEFVEVsFDS--LLTALKSGKIDVVAAGMTITPERAKQVDFSDPYYRSGQVIL-V 92
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     152 LHDSmrPLTSPKPVN---IARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSL 228
Cdd:smart00062   93 RKDS--PIKSLEDLKgkkVAVVAGTTAEELLKKLYPEAKIVSYDSNAEALAALKAGRADAAVADAPLLAALVKQHGLPEL 170
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 16130302     229 NVVKYYNSPRQYNFFLTRKESVILNEVLNRFVDAL-TNEVRYEVSQNWL 276
Cdd:smart00062  171 KIVPDPLDTPEGYAIAVRKGDPELLDKINKALKELkADGTLKKISEKWF 219
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
831-935 1.85e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 67.74  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  831 QVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTimDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKEL 910
Cdd:cd16921    3 QVLTNLLGNAIKFRRPRRPPRIEVGAEDVGEEWTFYVR--DNGIGIDPEYAEKVFGIFQRLHSREEYEGTGVGLAIVRKI 80
                         90       100
                 ....*....|....*....|....*
gi 16130302  911 IKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16921   81 IERHGGRIWLESEPGEGTTFYFTLP 105
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
961-1060 2.26e-13

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 67.19  E-value: 2.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTANA 1040
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREW-SAVPVIVLSARD 79
                         90       100
                 ....*....|....*....|
gi 16130302 1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:cd17620   80 EESDKIAALDAGADDYLTKP 99
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
830-935 2.99e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 67.04  E-value: 2.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  830 KQVLSNLLSNALKFTTEGAVK-----ITTSlghIDDNHAViKMTIMDSGSGLSQEEQQQLFKRYSQTSAgrqqTGSGLGL 904
Cdd:cd16920    2 QQVLINLVRNGIEAMSEGGCErreltIRTS---PADDRAV-TISVKDTGPGIAEEVAGQLFDPFYTTKS----EGLGMGL 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 16130302  905 MICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16920   74 SICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
958-1070 3.54e-13

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 69.60  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  958 KLSILIADDHPTNRLLLKRQLNLLGYDV-DEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNsSLPIWGL 1036
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEER-PAPVILL 81
                         90       100       110
                 ....*....|....*....|....*....|....
gi 16130302 1037 TANAQANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
Cdd:COG3707   82 TAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
PRK11517 PRK11517
DNA-binding response regulator HprR;
959-1098 5.83e-13

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 69.54  E-value: 5.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   959 LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSlPIWGLTA 1038
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT-PVICLTA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130302  1039 NAQANEREKGLSCGMNLCLFKPLTL-DVLKTHLSQL--HQVAHIAPQYRHLDIEALKNNTAND 1098
Cdd:PRK11517   80 RDSVDDRVRGLDSGANDYLVKPFSFsELLARVRAQLrqHHALNSTLEISGLRMDSVSQSVSRD 142
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
790-934 8.45e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 66.50  E-value: 8.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  790 TLVQNTCHSFGAIAASKSIALSCSstFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEgAVKITTslgHIDDNHAVIKmtI 869
Cdd:cd16954    1 PLLDSLCSALNKVYQRKGVSISLD--ISPELRFPGERNDLMELLGNLLDNACKWCLE-FVEVTA---RQTDGGLHLI--V 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  870 MDSGSGLSQEEQQQLFKRysQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI 934
Cdd:cd16954   73 DDDGPGVPESQRSKIFQR--GQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
825-925 1.19e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 65.17  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQVLSNLLSNALKFTTEGAVkITTSLgHIDDNHavIKMTIMDSGSGLSQEEQQQLFKR-YSQTSAGRQQTGSGLG 903
Cdd:cd16945    1 DPFLLRQAINNLLDNAIDFSPEGGL-IALQL-EADTEG--IELLVFDEGSGIPDYALNRVFERfYSLPRPHSGQKSTGLG 76
                         90       100
                 ....*....|....*....|..
gi 16130302  904 LMICKELIKNMQGDLSLESHPG 925
Cdd:cd16945   77 LAFVQEVAQLHGGRITLRNRPD 98
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
830-935 1.27e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 65.16  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  830 KQVLSNLLSNALKFTTeGAVKITTslghiDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKE 909
Cdd:cd16950    2 KRVLSNLVDNALRYGG-GWVEVSS-----DGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTSGTGLGLAIVQR 75
                         90       100
                 ....*....|....*....|....*.
gi 16130302  910 LIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16950   76 ISDAHGGSLTLANRAGGGLCARIELP 101
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
962-1060 1.56e-12

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 65.37  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  962 LIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPIWGLTAN 1039
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPktSSIPIIMLTAK 80
                         90       100
                 ....*....|....*....|.
gi 16130302 1040 AQANEREKGLSCGMNLCLFKP 1060
Cdd:cd19937   81 GEEFDKVLGLELGADDYITKP 101
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
313-519 1.74e-12

Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This group contains uncharacterized periplasmic cystine-binding domain of ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270431 [Multi-domain]  Cd Length: 218  Bit Score: 68.08  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  313 PPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVS-HNIHAGtqLSPGGWDIIPG--AIySEDRENNVLFAEAFITTP 389
Cdd:cd13713   11 PPFNFLDEDNQLVGFDVDVAKAIAKRLGVKVEPVTTAwDGIIAG--LWAGRYDIIIGsmTI-TEERLKVVDFSNPYYYSG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  390 YV-FVMQKAPDSEQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRYMIDHYYP 468
Cdd:cd13713   88 AQiFVRKDSTITSLADLKGKKVGVVTGTTYEAYARKYLPGAEIKTYDSDVLALQDLALGRLDAVITDRVTGLNAIKEGGL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302  469 N-----ELYHFLIPGVpnaslsfAFPRGEPELKDIINKALNAIPPSEVL-RLTEKWI 519
Cdd:cd13713  168 PikivgKPLYYEPMAI-------AIRKGDPELRAAVNKALAEMKADGTLeKISKKWF 217
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
825-932 1.98e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 64.73  E-value: 1.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQVLSNLLSNALKFTTEGA-VKITTSlghiDDNHAVIKmtIMDSGSGLSQEEQQQLFKRYSQtSAGRQQTGSGLG 903
Cdd:cd16940   10 DALLLFLLLRNLVDNAVRYSPQGSrVEIKLS----ADDGAVIR--VEDNGPGIDEEELEALFERFYR-SDGQNYGGSGLG 82
                         90       100
                 ....*....|....*....|....*....
gi 16130302  904 LMICKELIKNMQGDLSLESHPGIGTTFTI 932
Cdd:cd16940   83 LSIVKRIVELHGGQIFLGNAQGGGLEAWV 111
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
959-1066 2.02e-12

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 65.13  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  959 LSILIADDHPTNRLLLKRQLNLLGYDV-DEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSlPIWGLT 1037
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-PIVLLT 79
                         90       100
                 ....*....|....*....|....*....
gi 16130302 1038 ANAQANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd19932   80 AYSQQDLVERAKEAGAMAYLVKPFSESDL 108
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
959-1013 2.57e-12

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 62.59  E-value: 2.57e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 16130302     959 LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMP 1013
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
960-1033 2.67e-12

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 64.53  E-value: 2.67e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPI 1033
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPV 75
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
982-1060 4.54e-12

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 63.86  E-value: 4.54e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130302  982 GYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLReQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKP 1060
Cdd:cd17623   22 GFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR-KTSQVPVLMLTARGDDIDRILGLELGADDYLPKP 99
orf27 CHL00148
Ycf27; Reviewed
958-1066 4.84e-12

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 67.05  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   958 KLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLT 1037
Cdd:CHL00148    6 KEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE-SDVPIIMLT 84
                          90       100
                  ....*....|....*....|....*....
gi 16130302  1038 ANAQANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:CHL00148   85 ALGDVSDRITGLELGADDYVVKPFSPKEL 113
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
825-935 1.08e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 62.55  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQVLSNLLSNALKfTTEGA--VKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAgrqqTGSGL 902
Cdd:cd16944    1 DTTQISQVLTNILKNAAE-AIEGRpsDVGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPYVTTRP----KGTGL 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16130302  903 GLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16944   76 GLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
961-1060 1.13e-11

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 62.46  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTANA 1040
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK-STLPVIFLTSKD 79
                         90       100
                 ....*....|....*....|
gi 16130302 1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:cd19936   80 DEIDEVFGLRMGADDYITKP 99
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
959-1073 1.39e-11

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 62.55  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  959 LSILIADDHPTNRLLLKRQLNLlGYDVD--EATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGL 1036
Cdd:cd17593    1 MKVLICDDSSMARKQLARALPA-DWDVEitFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVV 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16130302 1037 TANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
Cdd:cd17593   80 SGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
961-1060 2.66e-11

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 61.88  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN--SSLPIWGLTA 1038
Cdd:cd17618    3 ILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEmtRDIPIIMLTA 82
                         90       100
                 ....*....|....*....|..
gi 16130302 1039 NAQANEREKGLSCGMNLCLFKP 1060
Cdd:cd17618   83 RGEEEDKVRGLEAGADDYITKP 104
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
961-1042 3.06e-11

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 61.36  E-value: 3.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKV-SMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTAN 1039
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81

                 ...
gi 16130302 1040 AQA 1042
Cdd:cd18160   82 AAA 84
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
957-1078 3.89e-11

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 66.59  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   957 EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGL 1036
Cdd:PRK10365    4 DNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIM 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 16130302  1037 TANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQlhQVAH 1078
Cdd:PRK10365   84 TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK--ALAH 123
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
832-935 3.90e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 60.76  E-value: 3.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  832 VLSNLLSNALKF---TTEGAVKITTSLGhiDDNHAVIkMTIMDSGSGLSQEEQQQLFKRYSQTSAgrqQTGSGLGLMICK 908
Cdd:cd16915    4 IVGNLIDNALDAlaaTGAPNKQVEVFLR--DEGDDLV-IEVRDTGPGIAPELRDKVFERGVSTKG---QGERGIGLALVR 77
                         90       100
                 ....*....|....*....|....*..
gi 16130302  909 ELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16915   78 QSVERLGGSITVESEPGGGTTFSIRIP 104
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
959-1061 8.11e-11

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 63.40  E-value: 8.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   959 LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTA 1038
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTA 80
                          90       100
                  ....*....|....*....|...
gi 16130302  1039 NAQANEREKGLSCGMNLCLFKPL 1061
Cdd:PRK09836   81 LGTIEHRVKGLELGADDYLVKPF 103
PRK13557 PRK13557
histidine kinase; Provisional
675-1045 8.55e-11

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 65.85  E-value: 8.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   675 ASDNAVYICGWQ-DITETRDLINAL-EVEKNKAIkatvakSQFLATMSHEIRTPISSIMGFLELLsGSGLSKE----QRV 748
Cdd:PRK13557  130 DAGDLVYFFGSQlDVSRRRDAEDALrQAQKMEAL------GQLTGGIAHDFNNLLQVMSGYLDVI-QAALSHPdadrGRM 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   749 --------EAISLAYATGQSLLGLigeildvdkieSGNYQLQPQWVDIPTLVQNTC----HSFG-AIAASKSIAlscsst 815
Cdd:PRK13557  203 arsvenirAAAERAATLTQQLLAF-----------ARKQRLEGRVLNLNGLVSGMGelaeRTLGdAVTIETDLA------ 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   816 fPEHYLVKIDPQAFKQVLSNLLSNALKFTTEGA-VKITTSLGHIDDN------------HAVIKMTimDSGSGLSQEEQQ 882
Cdd:PRK13557  266 -PDLWNCRIDPTQAEVALLNVLINARDAMPEGGrVTIRTRNVEIEDEdlamyhglppgrYVSIAVT--DTGSGMPPEILA 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   883 QLFKRYSQTS-AGRqqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEiSQQVATVEAKAEQPITLPEKLSI 961
Cdd:PRK13557  343 RVMDPFFTTKeEGK---GTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPAS-DQAENPEQEPKARAIDRGGTETI 418
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   962 LIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKV-SMQHYDLLITDVNMP-NMDGFELTRKLREQNSSLPIWGLTAN 1039
Cdd:PRK13557  419 LIVDDRPDVAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVLLTTGY 498

                  ....*..
gi 16130302  1040 AQAN-ER 1045
Cdd:PRK13557  499 AEASiER 505
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
832-935 9.90e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 59.99  E-value: 9.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  832 VLSNLLSNALKFTTEGAvKITTslgHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQ-QTGSGLGLMICKEL 910
Cdd:cd16948    9 IIGQIVSNALKYSKQGG-KIEI---YSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGRNfQESTGMGLYLVKKL 84
                         90       100
                 ....*....|....*....|....*
gi 16130302  911 IKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16948   85 CDKLGHKIDVESEVGEGTTFTITFP 109
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
961-1033 1.49e-10

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 60.20  E-value: 1.49e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPI 1033
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPV 73
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
832-937 1.55e-10

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 65.32  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   832 VLSNLLSNALKFTTEGAVK-ITTSLgHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKR-YSQTSAGRqqtgsGLGLMICKE 909
Cdd:PRK11086  437 ILGNLIENALEAVGGEEGGeISVSL-HYRNGWLHC--EVSDDGPGIAPDEIDAIFDKgYSTKGSNR-----GVGLYLVKQ 508
                          90       100
                  ....*....|....*....|....*...
gi 16130302   910 LIKNMQGDLSLESHPGIGTTFTITIPVE 937
Cdd:PRK11086  509 SVENLGGSIAVESEPGVGTQFFVQIPWD 536
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
961-1079 1.55e-10

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 59.87  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQ-LNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNS--SLPIWGLT 1037
Cdd:cd17552    4 ILVIDDEEDIREVVQAClEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPEtqSIPVILLT 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16130302 1038 ANAQANEREKGLSCGMNLCL---FKPLTLdvlkthlsqLHQVAHI 1079
Cdd:cd17552   84 AKAQPSDRQRFASLGVAGVIakpFDPLTL---------AEQIAKL 119
envZ PRK09467
osmolarity sensor protein; Provisional
716-937 1.58e-10

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 64.93  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   716 LATMSHEIRTPISSIMgflellsgsgLSKEQRVEaislayatGQSLL--GLIGEILDVDKIESG--NY-----QLQPQWV 786
Cdd:PRK09467  233 MAGVSHDLRTPLTRIR----------LATEMMSE--------EDGYLaeSINKDIEECNAIIEQfiDYlrtgqEMPMEMA 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   787 DIPTLVQNTCHSFGAIAASKSIALScsstfPEHYLVKIDPQAFKQVLSNLLSNALKFTTeGAVKITTSlghidDNHAVIK 866
Cdd:PRK09467  295 DLNALLGEVIAAESGYEREIETALQ-----PGPIEVPMNPIAIKRALANLVVNAARYGN-GWIKVSSG-----TEGKRAW 363
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302   867 MTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVE 937
Cdd:PRK09467  364 FQVEDDGPGIPPEQLKHLFQPFTRGDSARGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPLT 434
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
1102-1183 1.98e-10

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 58.55  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302 1102 MQEILMTFQHETHKDLPAAFQALE----AGDNRTFHQCIHRIHGAANILNLQKLINISHQLEIT--------PVSDDSKP 1169
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLeledAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLldalrdglEVTPELID 80
                         90
                 ....*....|....
gi 16130302 1170 EILQLLNSVKEHIA 1183
Cdd:cd00088   81 LLLDALDALKAELE 94
PRK10643 PRK10643
two-component system response regulator PmrA;
982-1067 2.09e-10

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 61.98  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   982 GYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPL 1061
Cdd:PRK10643   24 GYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTARDTLEDRVAGLDVGADDYLVKPF 103

                  ....*.
gi 16130302  1062 TLDVLK 1067
Cdd:PRK10643  104 ALEELH 109
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
304-519 2.36e-10

Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 periplasmic binding protein fold; This group includes the periplasmic substrate-binding protein ArtJ of the ATP-binding cassette (ABC) transport system from the thermophilic bacterium Geobacillus stearothermophilus, which is specific for arginine, lysine, and histidine. ArtJ belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270342 [Multi-domain]  Cd Length: 219  Bit Score: 61.74  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  304 LKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVshnihagtqlspgGWD-IIPG-------AIYS--- 372
Cdd:cd13624    2 LVVGTDATFPPFEFVDENGKIVGFDIDLIKAIAKEAGFEVEFKNM-------------AFDgLIPAlqsgkidIIISgmt 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  373 --EDRENNVLFAEAFITTPYVFVMQKAPDSEQTLK--KGMKVAIpyyyelhsQL--------KEMYPEVEWIQVDNASAA 440
Cdd:cd13624   69 itEERKKSVDFSDPYYEAGQAIVVRKDSTIIKSLDdlKGKKVGV--------QIgttgaeaaEKILKGAKVKRFDTIPLA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  441 FHKVKEGELDALVATQLNSRYMIDHyypNELYHFLIPGVPNAS--LSFAFPRGEPELKDIINKALNAIPPS-EVLRLTEK 517
Cdd:cd13624  141 FLELKNGGVDAVVNDNPVAAYYVKQ---NPDKKLKIVGDPLTSeyYGIAVRKGNKELLDKINKALKKIKENgTYDKIYKK 217

                 ..
gi 16130302  518 WI 519
Cdd:cd13624  218 WF 219
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
961-1033 2.53e-10

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 59.05  E-value: 2.53e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPI 1033
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPV 73
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
833-935 2.96e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 58.75  E-value: 2.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  833 LSNLLSNALKFTTEGavkittslGHI-----DDNHAViKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLM 905
Cdd:cd16952    5 FSNLVSNAVKYTPPS--------DTItvrwsQEESGA-RLSVEDTGPGIPPEHIPRLTERFYRvdIERCRNTGGTGLGLA 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 16130302  906 ICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16952   76 IVKHVMSRHDARLLIASELGKGSRFTCLFP 105
PRK10693 PRK10693
two-component system response regulator RssB;
987-1062 3.16e-10

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 62.70  E-value: 3.16e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302   987 EATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLT 1062
Cdd:PRK10693    2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVK 77
PRK10766 PRK10766
two-component system response regulator TorR;
960-1063 3.34e-10

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 61.21  E-value: 3.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTAN 1039
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSR-STVGIILVTGR 82
                          90       100
                  ....*....|....*....|....
gi 16130302  1040 AQANEREKGLSCGMNLCLFKPLTL 1063
Cdd:PRK10766   83 TDSIDRIVGLEMGADDYVTKPLEL 106
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
720-971 3.83e-10

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 64.31  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   720 SHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKieSGNYQLQPqwVDIPTLVQNtchsf 799
Cdd:PRK13837  458 AHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAGARARLIIDQILAFGR--KGERNTKP--FDLSELVTE----- 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   800 gaIAASKSIALSCSSTF-----PEHYLVKIDPQAFKQVLSNLLSNALK-FTTEGAVKIT---------TSLGHID---DN 861
Cdd:PRK13837  529 --IAPLLRVSLPPGVELdfdqdQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISlsraklrapKVLSHGVlppGR 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   862 HAVIKMTimDSGSGLSQEEQQQLFKRYSQTSAGrqqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQ 941
Cdd:PRK13837  607 YVLLRVS--DTGAGIDEAVLPHIFEPFFTTRAG----GTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVP 680
                         250       260       270
                  ....*....|....*....|....*....|
gi 16130302   942 VATVEAKAEQPITLPEKLSILIADDHPTNR 971
Cdd:PRK13837  681 VAPQAFFGPGPLPRGRGETVLLVEPDDATL 710
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
829-935 3.89e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 58.11  E-value: 3.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  829 FKQVLSNLLSNALKFTTEgAVKITTSlghIDDNHavIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQT--GSGLGLMI 906
Cdd:cd16949    1 LARALENVLRNALRYSPS-KILLDIS---QDGDQ--WTITITDDGPGVPEDQLEQIFLPFYRVDSARDREsgGTGLGLAI 74
                         90       100
                 ....*....|....*....|....*....
gi 16130302  907 CKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16949   75 AERAIEQHGGKIKASNRKPGGLRVRIWLP 103
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
831-919 4.08e-10

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 58.44  E-value: 4.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  831 QVLSNLLSNALKFTT--EGAVKITTSLG--HIDDNHAVIKMT--IMDSGSGLSQEEQQQLFKRysqtsaGRQQTGSGLGL 904
Cdd:cd16932    9 QVLADFLLNAVRFTPspGGWVEIKVSPTkkQIGDGVHVIHLEfrITHPGQGLPEELVQEMFEE------NQWTTQEGLGL 82
                         90
                 ....*....|....*
gi 16130302  905 MICKELIKNMQGDLS 919
Cdd:cd16932   83 SISRKLVKLMNGDVR 97
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
313-519 4.50e-10

Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 61.05  E-value: 4.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  313 PPYSMTDENGSVRGVMGDILNIITLQTG--LNFSPITVSHNIHAgtqLSPGGWD-IIPGAIYSEDRENNVLFAEAFITTP 389
Cdd:cd13629   11 PPFEMTDKKGELIGFDVDLAKALAKDLGvkVEFVNTAWDGLIPA---LQTGKFDlIISGMTITPERNLKVNFSNPYLVSG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  390 YVFVMQKAPDSEQTL-----KKGMKVAIpyyyEL----HSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQLnSR 460
Cdd:cd13629   88 QTLLVNKKSAAGIKSledlnKPGVTIAV----KLgttgDQAARKLFPKATILVFDDEAAAVLEVVNGKADAFIYDQP-TP 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  461 YMIDHYYPNELYHFLIPgVPNASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKWI 519
Cdd:cd13629  163 ARFAKKNDPTLVALLEP-FTYEPLGFAIRKGDPDLLNWLNNFLKQIKGDGTLdELYDKWF 221
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
961-1086 5.07e-10

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 63.33  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAYA 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 16130302  1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAPQYRHL 1086
Cdd:PRK11361   87 EVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHL 132
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
831-935 5.13e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 57.97  E-value: 5.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  831 QVLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVikmTIMDSGSGLSQEEQQQLFKR-YSQTSAGRQ-QTGSGLGLMICK 908
Cdd:cd16953    3 QVLRNLIGNAISFSPPDTGRITVSAMPTGKMVTI---SVEDEGPGIPQEKLESIFDRfYTERPANEAfGQHSGLGLSISR 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 16130302  909 ELIKNMQGDLSLESH--PG--IGTTFTITIP 935
Cdd:cd16953   80 QIIEAHGGISVAENHnqPGqvIGARFTVQLP 110
pleD PRK09581
response regulator PleD; Reviewed
961-1060 5.13e-10

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 63.38  E-value: 5.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSS--LPIWGLTA 1038
Cdd:PRK09581    5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATthIPVVMVTA 84
                          90       100
                  ....*....|....*....|..
gi 16130302  1039 NAQANEREKGLSCGMNLCLFKP 1060
Cdd:PRK09581   85 LDDPEDRVRGLEAGADDFLTKP 106
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
958-1027 7.91e-10

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 57.98  E-value: 7.91e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  958 KLSILIADDHPTNRLLLKRQ-LNLLGYDV-DEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL---REQ 1027
Cdd:COG2197    1 MIRVLIVDDHPLVREGLRALlEAEPDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLltpRER 75
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
959-1073 8.76e-10

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 57.84  E-value: 8.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  959 LSILIADDHPTNRLLLKRQLNLLGYD-VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSS---LPIW 1034
Cdd:cd17530    1 LRVLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNaavILMS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 16130302 1035 GLTANAQANEREKGLSCGMNL--CLFKPLTLDVLKTHLSQL 1073
Cdd:cd17530   81 GLDGGILESAETLAGANGLNLlgTLSKPFSPEELTELLTKY 121
ompR PRK09468
osmolarity response regulator; Provisional
961-1060 1.17e-09

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 59.99  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIMLTAKG 87
                          90       100
                  ....*....|....*....|
gi 16130302  1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:PRK09468   88 EEVDRIVGLEIGADDYLPKP 107
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
961-1060 1.30e-09

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 57.05  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTANA 1040
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT-SNVPIIMLTAKD 79
                         90       100
                 ....*....|....*....|
gi 16130302 1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:cd17614   80 SEVDKVLGLELGADDYVTKP 99
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
714-922 1.36e-09

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 62.40  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  714 QFLATMSHEIRTPISSIMGFLellsgsgLSKEQRVEAISLAYATgQSLLGLIGEILDVDKI--------ESGNYQLQPqw 785
Cdd:COG4192  435 QTMTSLAHELNQPLNAMSMYL-------FSAKKALEQENYAQLP-TSLDKIEGLIERMDKIikslrqfsRKSDTPLQP-- 504
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  786 VDIPTLVQntchSFGAIAASKSIALSCSSTFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEgAVKITTSLGHIDDNHAVi 865
Cdd:COG4192  505 VDLRQVIE----QAWELVESRAKPQQITLHIPDDLMVQGDQVLLEQVLVNLLVNALDAVAT-QPQISVDLLSNAENLRV- 578
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302  866 kmTIMDSGSGLSQEEqqQLFKRYSQTsagrQQTGSGLGLMICKELIKNMQGDLSLES 922
Cdd:COG4192  579 --AISDNGNGWPLVD--KLFTPFTTT----KEVGLGLGLSICRSIMQQFGGDLYLAS 627
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
832-935 1.49e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 56.24  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  832 VLSNLLSNALKFTTEGAVKITTSLghIDDNhaVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELI 911
Cdd:cd16923    4 VFSNLLSNAIKYSPENTRIYITSF--LTDD--VVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNTEGAGLGLSIAKAII 79
                         90       100
                 ....*....|....*....|....
gi 16130302  912 KNMQGDLSLESHpGIGTTFTITIP 935
Cdd:cd16923   80 ELHGGSASAEYD-DNHDLFKVRLP 102
PRK10336 PRK10336
two-component system response regulator QseB;
982-1085 1.98e-09

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 59.14  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   982 GYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPL 1061
Cdd:PRK10336   24 GFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTARDALAERVEGLRLGADDYLCKPF 103
                          90       100
                  ....*....|....*....|....*.
gi 16130302  1062 TLDVLKTHLSQLHQVAH--IAPQYRH 1085
Cdd:PRK10336  104 ALIEVAARLEALMRRTNgqASNELRH 129
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
961-1066 3.07e-09

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 55.88  E-value: 3.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100
                 ....*....|....*....|....*.
gi 16130302 1041 QANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDEL 106
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
364-520 6.15e-09

The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270230 [Multi-domain]  Cd Length: 223  Bit Score: 57.61  E-value: 6.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  364 DII-PGAIYSEDRENNVLFAEAFITTPYVFVMQK---APDSEQTLKkGMKVAIPY---YYELHSQLKEMYPEVEWIQVDN 436
Cdd:cd01009   61 DLAaAGLTITPERKKKVDFSFPYYYVVQVLVYRKgspRPRSLEDLS-GKTIAVRKgssYAETLQKLNKGGPPLTWEEVDE 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  437 ASAA--FHKVKEGELDALVA----TQLNSRymidhYYPNELYHFLIPgvPNASLSFAFPRGEPELKDIINKALNAIPPSE 510
Cdd:cd01009  140 ALTEelLEMVAAGEIDYTVAdsniAALWRR-----YYPELRVAFDLS--EPQPLAWAVRKNSPSLLAALNRFLAQIKKDG 212
                        170
                 ....*....|.
gi 16130302  511 VL-RLTEKWIK 520
Cdd:cd01009  213 TLaRLYERYYG 223
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
356-520 7.49e-09

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 59.31  E-value: 7.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  356 TQLSPGGWDII-PGAIYSEDRENNVLFAEAFITTPYVFVMQKAPDSEQTLK--KGMKVAIP---YYYELHSQLKEMYPEV 429
Cdd:COG4623   74 PALNAGEGDIAaAGLTITPERKKQVRFSPPYYSVSQVLVYRKGSPRPKSLEdlAGKTVHVRagsSYAERLKQLNQEGPPL 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  430 EWIQVDNASAA--FHKVKEGELDALVATQlNSRYMIDHYYPNELYHFLIPgvPNASLSFAFPRGEPELKDIINKALNAIP 507
Cdd:COG4623  154 KWEEDEDLETEdlLEMVAAGEIDYTVADS-NIAALNQRYYPNLRVAFDLS--EPQPIAWAVRKNDPSLLAALNEFFAKIK 230
                        170
                 ....*....|....
gi 16130302  508 PSEVL-RLTEKWIK 520
Cdd:COG4623  231 KGGTLaRLYERYFG 244
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
961-1060 8.77e-09

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 54.27  E-value: 8.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKV-SMQHYDLLITDVNMPN-MDGFELTRKLREQNSSLPIWGLTA 1038
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLeSGPDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSG 80
                         90       100
                 ....*....|....*....|..
gi 16130302 1039 NAQANEREKGLSCGMNLcLFKP 1060
Cdd:cd18161   81 YAENAIEGGDLAPGVDV-LSKP 101
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
953-1098 9.80e-09

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 56.96  E-value: 9.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   953 ITLPEKLSILIADDHPTNRL-LLKRQLNLLGYD-VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSS 1030
Cdd:PRK10651    1 MSNQEPATILLIDDHPMLRTgVKQLISMAPDITvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130302  1031 LPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLkthLSQLHQVAH----IAPQYRHLDIEALKNNTAND 1098
Cdd:PRK10651   81 GRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDL---LKALQQAAAgemvLSEALTPVLAASLRANRATT 149
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
960-1060 1.10e-08

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 54.30  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTAN 1039
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH-SHVPILMLTAR 79
                         90       100
                 ....*....|....*....|.
gi 16130302 1040 AQANEREKGLSCGMNLCLFKP 1060
Cdd:cd19939   80 TEEMDRVLGLEMGADDYLCKP 100
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
76-375 1.47e-08

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 58.53  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   76 QQRVRGINADYLNLLKRALNIKLTLREYADHQKAMDALAEGEVDIVLSHLVTSPPLNNDIAATKPLIITFPALVTtlHDS 155
Cdd:COG4623   39 RGGPMGFEYELAKAFADYLGVKLEIIVPDNLDELLPALNAGEGDIAAAGLTITPERKKQVRFSPPYYSVSQVLVY--RKG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  156 MRPLTSP-----KPVNIARVANYPPD-EVIHQSFPKATIISFTNL--YQALASVSAGHNDYFIG-SNIItsSMISRYFTH 226
Cdd:COG4623  117 SPRPKSLedlagKTVHVRAGSSYAERlKQLNQEGPPLKWEEDEDLetEDLLEMVAAGEIDYTVAdSNIA--ALNQRYYPN 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  227 sLNVVKYYNSPRQYNFFLtRKESVILNEVLNRFVDALTNEVRYEVSQN----WLDTGNLAFLNKPLELTEHEKQWIKQH- 301
Cdd:COG4623  195 -LRVAFDLSEPQPIAWAV-RKNDPSLLAALNEFFAKIKKGGTLARLYEryfgHVKRDTRAFLRRIEGRLPPYDPLFEKYa 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  302 -------PNLKVL---E---NPY--SPpysmtdenGSVRGVMGdilniITLQTGLNF------SPITvshNIHAGT---- 356
Cdd:COG4623  273 eeygldwRLLAALayqEshwNPRarSP--------TGARGLMQ-----LMPATAKELgvddrlDPEQ---SIRAGAkylr 336
                        330
                 ....*....|....*....
gi 16130302  357 QLspggWDIIPGAIYSEDR 375
Cdd:COG4623  337 WL----YDRFPEAIDEPDR 351
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
985-1033 1.84e-08

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 53.93  E-value: 1.84e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 16130302  985 VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNsSLPI 1033
Cdd:cd17541   29 VGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAER-PTPV 76
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
831-935 1.85e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 53.56  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  831 QVLSNLLSNALKFT--TEGAVKITTS------LGHiDDNHAVIKMTIMDSGSGLSQEEQQQLFkrYSQTSaGRQQtGSGL 902
Cdd:cd16918    3 QVFLNLVRNAAQALagSGGEIILRTRtqrqvtLGH-PRHRLALRVSVIDNGPGIPPDLQDTIF--YPMVS-GREN-GTGL 77
                         90       100       110
                 ....*....|....*....|....*....|...
gi 16130302  903 GLMICKELIKNMQGDLSLESHPGiGTTFTITIP 935
Cdd:cd16918   78 GLAIAQNIVSQHGGVIECDSQPG-HTVFSVSLP 109
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
982-1052 2.40e-08

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 56.12  E-value: 2.40e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302   982 GYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCG 1052
Cdd:PRK11083   27 GFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTARSDEVDRLVGLEIG 97
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
304-506 2.84e-08

Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 periplasmic binding protein fold; This subgroup includes the periplasmic binding component of ABC transporter involved in uptake of mimosine MidA and its similar proteins. This periplasmic binding domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270225 [Multi-domain]  Cd Length: 230  Bit Score: 55.71  E-value: 2.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  304 LKVLENPYSPPYSMTDENGSVRGVMGDILNII--TLQTGLNFSPITVSHNIHAgtqLSPGGWDIIPGAIY-SEDRENNVL 380
Cdd:cd01004    4 LTVGTNPTYPPYEFVDEDGKLIGFDVDLAKAIakRLGLKVEIVNVSFDGLIPA---LQSGRYDIIMSGITdTPERAKQVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  381 FAEAFITTPYVFVMQKAPDSEQTLK--KGMKVAIP--YYYELHSQ------LKEMYPEVEWIQVDNASAAFHKVKEGELD 450
Cdd:cd01004   81 FVDYMKDGLGVLVAKGNPKKIKSPEdlCGKTVAVQtgTTQEQLLQaankkcKAAGKPAIEIQTFPDQADALQALRSGRAD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302  451 ALVATQLNSRYMIDHYyPNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAI 506
Cdd:cd01004  161 AYLSDSPTAAYAVKQS-PGKLELVGEVFGSPAPIGIAVKKDDPALADAVQAALNAL 215
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
961-1067 3.32e-08

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 52.94  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAYG 82
                         90       100
                 ....*....|....*....|....*..
gi 16130302 1041 QANEREKGLSCGMNLCLFKPLTLDVLK 1067
Cdd:cd17553   83 ELDMIQESKELGALTHFAKPFDIDEIR 109
glnL PRK11073
nitrogen regulation protein NR(II);
824-936 3.61e-08

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 57.01  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   824 IDPQAFKQVLSNLLSNALKFTTE--GAVKITTSLGHIDDNHA-----VIKMTIMDSGSGLSQEEQQQLFkrYSQTSaGRQ 896
Cdd:PRK11073  233 HDPDQIEQVLLNIVRNALQALGPegGTITLRTRTAFQLTLHGeryrlAARIDIEDNGPGIPPHLQDTLF--YPMVS-GRE 309
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 16130302   897 qTGSGLGLMICKELIKNMQGDLSLESHPGiGTTFTITIPV 936
Cdd:PRK11073  310 -GGTGLGLSIARNLIDQHSGKIEFTSWPG-HTEFSVYLPI 347
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
960-1038 3.97e-08

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 52.66  E-value: 3.97e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTA 1038
Cdd:cd19919    2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
961-1060 4.40e-08

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 52.38  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLReQNSSLPIWGLTANA 1040
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIR-RFSDVPIIMVTARV 80
                         90       100
                 ....*....|....*....|
gi 16130302 1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:cd19938   81 EEIDRLLGLELGADDYICKP 100
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
961-1062 8.49e-08

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 51.38  E-value: 8.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                         90       100
                 ....*....|....*....|..
gi 16130302 1041 QANEREKGLSCGMnlclFKPLT 1062
Cdd:cd19926   81 SLDTAIEALKAGA----FDFLT 98
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
958-1041 1.03e-07

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 54.05  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  958 KLSILIADDHPTNRLLLKRQ-LNLLGYD-VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWG 1035
Cdd:COG3279    1 MMKILIVDDEPLARERLERLlEKYPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80

                 ....*.
gi 16130302 1036 LTANAQ 1041
Cdd:COG3279   81 TTAYDE 86
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
960-1027 1.29e-07

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 51.25  E-value: 1.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQ 1027
Cdd:cd17569    2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRER 69
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
714-942 1.31e-07

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 54.97  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   714 QFLATMSHEIRTPISSIMGFLELLSGSGLSKEQR-VEAISLAYATGQSLLGL--IGEildvdKIESGNYQlQPQWV-DIP 789
Cdd:PRK10755  139 LFTADVAHELRTPLAGIRLHLELLEKQHHIDVAPlIARLDQMMHTVEQLLQLarAGQ-----SFSSGHYQ-TVKLLeDVI 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   790 TLVQNtchSFGAIAASKSIALSCSSTFPEHYlVKIDPQAFKQVLSNLLSNALKFTTEGAvKITTSLGHIDDNhavIKMTI 869
Cdd:PRK10755  213 LPSQD---ELSEMLEQRQQTLLLPESAADIT-VQGDATLLRLLLRNLVENAHRYSPEGS-TITIKLSQEDGG---AVLAV 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   870 MDSGSGLSQEEQQQLFK-------RYSqtsagrqqtGSGLGLMICKELIKNMQGDLSLESHP-GIGTTFTITIPVEISQQ 941
Cdd:PRK10755  285 EDEGPGIDESKCGELSKafvrmdsRYG---------GIGLGLSIVSRITQLHHGQFFLQNRQeRSGTRAWVWLPKAQNVA 355

                  .
gi 16130302   942 V 942
Cdd:PRK10755  356 N 356
PRK11173 PRK11173
two-component response regulator; Provisional
961-1060 1.43e-07

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 53.87  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWgLTanA 1040
Cdd:PRK11173    6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQANVALMF-LT--G 82
                          90       100
                  ....*....|....*....|..
gi 16130302  1041 QANEREK--GLSCGMNLCLFKP 1060
Cdd:PRK11173   83 RDNEVDKilGLEIGADDYITKP 104
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
846-937 1.85e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 55.02  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  846 EGAVKITtslGHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSAGRqqtgsGLGLMICKELIKNMQGD---LSLES 922
Cdd:COG2972  359 GGTIRIS---IRKEGDRLVI--TVEDNGVGMPEEKLEKLLEELSSKGEGR-----GIGLRNVRERLKLYYGEeygLEIES 428
                         90
                 ....*....|....*
gi 16130302  923 HPGIGTTFTITIPVE 937
Cdd:COG2972  429 EPGEGTTVTIRIPLE 443
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
961-1041 1.91e-07

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 50.74  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYD-VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTAN 1039
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILTKAGYEvVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSAM 82

                 ..
gi 16130302 1040 AQ 1041
Cdd:cd17542   83 GQ 84
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
829-935 2.01e-07

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 50.84  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  829 FKQVLSNLLSNALKFTTEGA-VKITTSLGHIDDNHAV----------IKMTIMDSGSGLSQEEQQQLFKRYSQTSA-GRq 896
Cdd:cd16919    1 LELAILNLAVNARDAMPEGGrLTIETSNQRVDADYALnyrdlipgnyVCLEVSDTGSGMPAEVLRRAFEPFFTTKEvGK- 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16130302  897 qtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16919   80 --GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
PBP2_Arg_STM4351 cd13700
Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding ...
313-518 2.48e-07

Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding protein fold; This group includes domains similar to Escherichia coli arginine third transport system. STM4351 is the high arginine specific periplasmic-binding protein of ABC transport system. STM4351 belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270418 [Multi-domain]  Cd Length: 222  Bit Score: 52.83  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  313 PPYSMTDENGSVRGVMGDILNIITLQtglnfspitvshnIHAGTQLSPGGWD-IIPG-------AIYS-----EDRENNV 379
Cdd:cd13700   13 PPFESIGAKGEIVGFDIDLANALCKQ-------------MQAECTFTNQAFDsLIPSlkfkkfdAVISgmditPEREKQV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  380 LFAEAFITTPYVFVMQKAPDSEQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVA-TQLN 458
Cdd:cd13700   80 SFSTPYYENSAVVIAKKDTYKTFADLKGKKIGVQNGTTHQKYLQDKHKEITTVSYDSYQNAFLDLKNGRIDGVFGdTAVV 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302  459 SRYMIDhyypNELYHFLIPGV--PN---ASLSFAFPRGEPELKDIINKALNAIPPS-EVLRLTEKW 518
Cdd:cd13700  160 AEWLKT----NPDLAFVGEKVtdPNyfgTGLGIAVRKDNQALLEKLNAALAAIKANgEYQKIYDKW 221
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
745-937 2.75e-07

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 54.53  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  745 EQRVEAISLAYatgqsllgligEILdvdkIESGNYQLqpqwVDIPTLVQNTCHSFGAIAASKSIALSCSSTFpehylVKI 824
Cdd:COG3920  337 QNRIQALALVH-----------ELL----YQSEDWEG----VDLRDYLRELLEPLRDSYGGRGIRIELDGPD-----VEL 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQ---VLSNLLSNALK--FTTEGAVKITTSLgHIDDNHAVIkmTIMDSGSGLSQEEQQQlfkrysqtsagrqqTG 899
Cdd:COG3920  393 PADAAVPlglILNELVTNALKhaFLSGEGGRIRVSW-RREDGRLRL--TVSDNGVGLPEDVDPP--------------AR 455
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 16130302  900 SGLGLMICKELIKNMQGDLSLESHPgiGTTFTITIPVE 937
Cdd:COG3920  456 KGLGLRLIRALVRQLGGTLELDRPE--GTRVRITFPLA 491
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
825-934 5.74e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 49.00  E-value: 5.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQVLSNLLSNALKFTTEGAvkiTTSLgHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTG-SGLG 903
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGG---TVSI-SIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGhYGMG 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 16130302  904 LMICKELIKNMQGDLSLESHPGIGTTFTITI 934
Cdd:cd16975   77 LYIAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
304-518 6.25e-07

Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic binding protein fold; This group contains cystine binding domain FliY and its related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270430 [Multi-domain]  Cd Length: 219  Bit Score: 51.62  E-value: 6.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  304 LKV-LENPYsPPYSMTDENGSVRGVMGDILNIITLQTGLN--FSPITVSHnIHAGtqLSPGGWDIIPGAI-YSEDRENNV 379
Cdd:cd13712    2 LRIgLEGTY-PPFNFKDETGQLTGFEVDVAKALAAKLGVKpeFVTTEWSG-ILAG--LQAGKYDVIINQVgITPERQKKF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  380 LFAEAF-ITTPYVFVMQKAPDSEQTLK--KGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALvatq 456
Cdd:cd13712   78 DFSQPYtYSGIQLIVRKNDTRTFKSLAdlKGKKVGVGLGTNYEQWLKSNVPGIDVRTYPGDPEKLQDLAAGRIDAA---- 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  457 LNSRYMIDhYYPNELYHFLIPG--VPNASLSFAFPRGEPELKDIINKALNAIPPSEVL-RLTEKW 518
Cdd:cd13712  154 LNDRLAAN-YLVKTSLELPPTGgaFARQKSGIPFRKGNPKLKAAINKAIEDLRADGTLaKLSEKW 217
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
832-936 8.87e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 48.58  E-value: 8.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  832 VLSNLLSNALKFTtegAVKITTSLgHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKE 909
Cdd:cd16939    4 ALDNLLRNALRYA---HRTVRIAL-LVSGGRLTL--IVEDDGPGIPAAARERVFEPFVRldPSRDRATGGFGLGLAIVHR 77
                         90       100
                 ....*....|....*....|....*..
gi 16130302  910 LIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:cd16939   78 VALWHGGHVECDDSELGGACFRLTWPR 104
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
961-1060 9.07e-07

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 49.01  E-value: 9.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTANA 1040
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE-SGVPIVMLTAKS 81
                         90       100
                 ....*....|....*....|
gi 16130302 1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:cd17626   82 DTVDVVLGLESGADDYVAKP 101
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
961-1045 1.38e-06

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 47.88  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVdEATDGVQALHK-VSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTAN 1039
Cdd:cd19928    1 ILVADDDRAIRTVLTQALGRAGYEV-RTTGNAATLWRwVEEGEGDLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQ 79
                         90
                 ....*....|..
gi 16130302 1040 ------AQANER 1045
Cdd:cd19928   80 ntlmtaVKAAER 91
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
960-1074 1.56e-06

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 48.57  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLG--YDVDEATDGVQALH-------KVSMQHYDLLITDVNMPNMDGFELTRKLREQNS- 1029
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDflrgegeYADAPRPDLILLDLNMPRMDGFEVLREIKADPDl 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 16130302 1030 -SLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLH 1074
Cdd:cd17557   81 rRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLG 126
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
74-276 1.98e-06

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 49.98  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302     74 DSQQRVRGINADYLNLLKRALNIKLTLReYADHQKAMDALAEGEVDIVLSHLVTSPPLNNDIAATKPLIITFPALVTTLH 153
Cdd:pfam00497   16 DENGKLVGFDVDLAKAIAKRLGVKVEFV-PVSWDGLIPALQSGKVDLIIAGMTITPERAKQVDFSDPYYYSGQVILVRKK 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302    154 DSMRPLTSP---KPVNIARVANYPPDEVIHQ-SFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFTHSLN 229
Cdd:pfam00497   95 DSSKSIKSLadlKGKTVGVQKGSTAEELLKNlKLPGAEIVEYDDDAEALQALANGRVDAVVADSPVAAYLIKKNPGLNLV 174
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 16130302    230 VVKYYNSPRQYNFFLTRKESVILNEVlNRFVDALTNEVRY-EVSQNWL 276
Cdd:pfam00497  175 VVGEPLSPEPYGIAVRKGDPELLAAV-NKALAELKADGTLaKIYEKWF 221
PBP2_Ehub_like cd01002
Substrate binding domain of ectoine/hydroxyectoine specific ABC transport system; the type 2 ...
313-518 2.61e-06

Substrate binding domain of ectoine/hydroxyectoine specific ABC transport system; the type 2 periplasmic binding protein fold; This family represents the periplasmic substrate-binding component of ABC transport systems that involved in uptake of osmoprotectants (also termed compatible solutes) such as ectoine and hydroxyectoine. To counteract the efflux of water, bacteria and archaea accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270223 [Multi-domain]  Cd Length: 242  Bit Score: 49.97  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  313 PPYSMTDENGSVRGVMGDILNIITLQTG---LNFSPITVSHNIHAgtqLSPGGWDII-PGAIYSEDRENNVLFAEAFITT 388
Cdd:cd01002   20 PPYAYIDADGEVTGESPEVARAVLKRLGvddVEGVLTEFGSLIPG---LQAGRFDVIaAGMFITPERCEQVAFSEPTYQV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  389 PYVFVMQKA-P---DSEQTLKK--GMKVAIPYYYELHSQLKEM-YPEVEWIQVDNASAAFHKVKEGELDALVATQLNSRY 461
Cdd:cd01002   97 GEAFLVPKGnPkglHSYADVAKnpDARLAVMAGAVEVDYAKASgVPAEQIVIVPDQQSGLAAVRAGRADAFALTALSLRD 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130302  462 MIDHYYPNEL---YHFL--IPGVPNASLS-FAFPRGEPELKDIINKALNAIPPS-EVLRLTEKW 518
Cdd:cd01002  177 LAAKAGSPDVevaEPFQpvIDGKPQIGYGaFAFRKDDTDLRDAFNAELAKFKGSgEHLEILEPF 240
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
814-935 2.80e-06

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 51.47  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   814 STFPEHYLVKIDPQAFKQVLSNLLSNALKFTTEgavKITTSLgHIDDNHAVIkmTIMDSGSGLSQEEQQQLFKRYSQTSA 893
Cdd:PRK09470  339 SAPPGPWPINGNPNALASALENIVRNALRYSHT---KIEVAF-SVDKDGLTI--TVDDDGPGVPEEEREQIFRPFYRVDE 412
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 16130302   894 GR--QQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:PRK09470  413 ARdrESGGTGLGLAIVENAIQQHRGWVKAEDSPLGGLRLTIWLP 456
PRK10816 PRK10816
two-component system response regulator PhoP;
961-1064 3.30e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 49.35  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:PRK10816    3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARE 82
                          90       100
                  ....*....|....*....|....
gi 16130302  1041 QANEREKGLSCGMNLCLFKPLTLD 1064
Cdd:PRK10816   83 SWQDKVEVLSAGADDYVTKPFHIE 106
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
957-1073 5.29e-06

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 46.60  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  957 EKLSILIADdhptnrlllkrQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGL 1036
Cdd:cd17622   10 PKLARLIAD-----------FLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK-YQGPILLL 77
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 16130302 1037 TANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
Cdd:cd17622   78 TALDSDIDHILGLELGADDYVVKPVEPAVLLARLRAL 114
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
959-1072 5.90e-06

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 46.47  E-value: 5.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  959 LSILIADDHP-TNRLLLKRQLNLLGYDV-DEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGL 1036
Cdd:cd19925    1 INVLIVEDDPmVAEIHRAYVEQVPGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVV 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 16130302 1037 TANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQ 1072
Cdd:cd19925   81 TAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
961-1060 5.95e-06

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 46.04  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLReQNSSLPIWGLTANA 1040
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR-ARSNVPVIMVTAKD 79
                         90       100
                 ....*....|....*....|
gi 16130302 1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
956-1033 6.71e-06

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 47.99  E-value: 6.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130302  956 PEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPI 1033
Cdd:COG4567    2 AEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARI 79
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
985-1029 7.28e-06

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 46.11  E-value: 7.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 16130302  985 VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNS 1029
Cdd:cd19930   27 VAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELP 71
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
965-1060 7.96e-06

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 45.82  E-value: 7.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  965 DDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNS--SLPIWGLTANAQA 1042
Cdd:cd17602    5 DDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSAlkDTPIIMLTGKDGL 84
                         90
                 ....*....|....*...
gi 16130302 1043 NEREKGLSCGMNLCLFKP 1060
Cdd:cd17602   85 VDRIRAKMAGASGYLTKP 102
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
73-275 8.04e-06

The substrate binding domain of putative amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Agrobacterium tumefaciens and its related proteins. The putative Atu4678-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270414 [Multi-domain]  Cd Length: 227  Bit Score: 48.53  E-value: 8.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   73 TDSQQRVRGINADYLNLLKRALNIKLTLREyADHQKAMDALAEGEVDIVLSHLVTSPPLNNDIAATKPLIITFPALVT-- 150
Cdd:cd13696   24 RDAAGNPVGYDVDYAKDLAKALGVKPEIVE-TPSPNRIPALVSGRVDVVVANTTRTLERAKTVAFSIPYVVAGMVVLTrk 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  151 -----TLHDsmrpLTSPKpvnIARVANYPPDEVIHQSFPKATIISFTNLYQALASVSAGHNDYFIGSNIITSSMISRYFT 225
Cdd:cd13696  103 dsgikSFDD----LKGKT---VGVVKGSTNEAAVRALLPDAKIQEYDTSADAILALKQGQADAMVEDNTVANYKASSGQF 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16130302  226 HSLNVVKYYNSPRQYNFFLTRKESVILNEVLNRFVDALTNEVRY-EVSQNW 275
Cdd:cd13696  176 PSLEIAGEAPYPLDYVAIGVRKGDYDWLRYLNLFVFQQNASGRYaELYQKW 226
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
961-1028 9.36e-06

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 45.99  E-value: 9.36e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGY--DVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN 1028
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDieIVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLA 70
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
1104-1188 9.53e-06

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 45.03  E-value: 9.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   1104 EILMTFQHETHKDLPAAFQALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLEiTPVSDDSKPEILQLLNSVKEHIA 1183
Cdd:pfam01627    1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELE-DLLREGELPLDPELLEALRDLLE 79

                   ....*
gi 16130302   1184 ELDQE 1188
Cdd:pfam01627   80 ALRAA 84
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
716-924 9.81e-06

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 49.63  E-value: 9.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   716 LATMSHEIRTPISSIMGFLE-LLSGSGLSKEQrVEAISLAYATGQSllGLIGEILDVDKIESGNYQLQPQWVDIPTLVQN 794
Cdd:PRK10815  270 LTDLTHSLKTPLAVLQSTLRsLRSGKQMSVEQ-AEPIMLEQISRIS--QQIGYYLHRASMRSEHNLLSRELHSVAPLLDN 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   795 TCHSFGAIAASKSIALSCSSTfPEHYLV--KIDpqaFKQVLSNLLSNALKFTTEgAVKITTslgHIDDNHAVIkmTIMDS 872
Cdd:PRK10815  347 LTSALNKVYQRKGVNITLDIS-PEITFVgeKND---FMEVMGNVLDNACKYCLE-FVEISA---RQTDEHLHI--VVEDD 416
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16130302   873 GSGLSQEEQQQLFKRysQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHP 924
Cdd:PRK10815  417 GPGIPESKRELIFDR--GQRADTLRPGQGLGLSVAREITEQYEGKISAGDSP 466
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
961-1060 1.14e-05

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 47.88  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSmQHYDLLITDVNMPNMDGFELTRKLReQNSSLPIWGLTANA 1040
Cdd:PRK10955    4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELR-QTHQTPVIMLTARG 81
                          90       100
                  ....*....|....*....|
gi 16130302  1041 QANEREKGLSCGMNLCLFKP 1060
Cdd:PRK10955   82 SELDRVLGLELGADDYLPKP 101
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
961-1063 1.38e-05

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 45.52  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLReQNSSLPIWGLTANA 1040
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIR-ARSDVPIIIISGDR 80
                         90       100
                 ....*....|....*....|....
gi 16130302 1041 -QANEREKGLSCGMNLCLFKPLTL 1063
Cdd:cd17594   81 rDEIDRVVGLELGADDYLAKPFGL 104
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
364-518 1.47e-05

Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; This periplasmic substrate-binding component serves as an initial receptor in the ABC transport of glutamine in bacteria and eukaryota. GlnH belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270216 [Multi-domain]  Cd Length: 218  Bit Score: 47.66  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  364 DIIPGAIY-SEDRENNVLFAEafittPY----VFVMQKAPDSE-QTLK--KGMKVAIPYYYELHSQLKEMYPEVEWIQVD 435
Cdd:cd00994   60 DIAIAGITiTEERKKVVDFSD-----PYydsgLAVMVKADNNSiKSIDdlAGKTVAVKTGTTSVDYLKENFPDAQLVEFP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  436 NASAAFHKVKEGELDALVatqlnsrymidHYYPNELYHFLIPGVPN-----ASLS-----FAFPRGEpELKDIINKALNA 505
Cdd:cd00994  135 NIDNAYMELETGRADAVV-----------HDTPNVLYYAKTAGKGKvkvvgEPLTgeqygIAFPKGS-ELREKVNAALKT 202
                        170
                 ....*....|....
gi 16130302  506 IPPS-EVLRLTEKW 518
Cdd:cd00994  203 LKADgTYDEIYKKW 216
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
831-932 1.52e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 44.76  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  831 QVLSNLLSNALKFTTEGAV-KITTSLGHIDDNhavIKMTIMDSGSGLSQEEQQQLFKRYSQTS-AGRqqtGSGLGLMICK 908
Cdd:cd16976    3 QVLMNLLQNALDAMGKVENpRIRIAARRLGGR---LVLVVRDNGPGIAEEHLSRVFDPFFTTKpVGK---GTGLGLSISY 76
                         90       100
                 ....*....|....*....|....
gi 16130302  909 ELIKNMQGDLSLESHPGIGTTFTI 932
Cdd:cd16976   77 GIVEEHGGRLSVANEEGAGARFTF 100
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
982-1033 2.11e-05

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 46.63  E-value: 2.11e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16130302  982 GYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPI 1033
Cdd:COG4566   23 GLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPV 74
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
312-520 2.19e-05

Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold; This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270407 [Multi-domain]  Cd Length: 229  Bit Score: 47.23  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  312 SPPYSMTDE-NGSVRGVMGDILNII--TLQTGLNFSPITVSHNIhagTQLSPGGWDIIPGAI-YSEDRENNVLFAEAFIT 387
Cdd:cd13689   18 VPPFGFIDPkTREIVGFDVDLCKAIakKLGVKLELKPVNPAARI---PELQNGRVDLVAANLtYTPERAEQIDFSDPYFV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  388 TPYVFVMQK-APDSEQTLKKGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVA-TQLNSRYMIDH 465
Cdd:cd13689   95 TGQKLLVKKgSGIKSLKDLAGKRVGAVKGSTSEAAIREKLPKASVVTFDDTAQAFLALQQGKVDAITTdETILAGLLAKA 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130302  466 YYPNELyhflipGVPNASLS-----FAFPRGEPELKDIINKALNAIPPS-EVLRLTEKWIK 520
Cdd:cd13689  175 PDPGNY------EILGEALSyepygIGVPKGESALRDFVNETLADLEKDgEADKIYDKWFG 229
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
298-525 2.21e-05

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 47.41  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   298 IKQHPNLKV-LENPYsPPYSMTDENGSVRGVMGDILNIITLQTGLNfspitvshnihagTQLSPGGWDIIPGAI------ 370
Cdd:PRK11260   37 VKERGTLLVgLEGTY-PPFSFQGEDGKLTGFEVEFAEALAKHLGVK-------------ASLKPTKWDGMLASLdskrid 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   371 -------YSEDRENNVLFaeafiTTPY------VFVMQKAPDSEQTLK--KGMKVAIPYYYELHSQLKEMYPEVEWIQVD 435
Cdd:PRK11260  103 vvinqvtISDERKKKYDF-----STPYtvsgiqALVKKGNEGTIKTAAdlKGKKVGVGLGTNYEQWLRQNVQGVDVRTYD 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   436 NASAAFHKVKEGELDALVATQLNSRYMIDHYyPNELyhfLIPGVPNASLS--FAFPRGEPELKDIINKALNAIPPSEVL- 512
Cdd:PRK11260  178 DDPTKYQDLRVGRIDAILVDRLAALDLVKKT-NDTL---AVAGEAFSRQEsgVALRKGNPDLLKAVNQAIAEMQKDGTLk 253
                         250
                  ....*....|...
gi 16130302   513 RLTEKWIKMpNVT 525
Cdd:PRK11260  254 ALSEKWFGA-DVT 265
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1006-1040 2.29e-05

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 44.89  E-value: 2.29e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 16130302 1006 LITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:cd17537   48 LVLDVRMPGMSGLELQDELLARGSNIPIIFITGHG 82
PRK15115 PRK15115
response regulator GlrR; Provisional
960-1081 2.47e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 48.29  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTAN 1039
Cdd:PRK15115    7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAH 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 16130302  1040 AQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQlhQVAHIAP 1081
Cdd:PRK15115   87 GSIPDAVAATQQGVFSFLTKPVDRDALYKAIDD--ALEQSAP 126
fixJ PRK09390
response regulator FixJ; Provisional
956-1033 3.54e-05

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 46.15  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   956 PEKLSILIADDHPTNRLLLKRQLNLLGYDV---DEATDGVQALHKVSmqhYDLLITDVNMPNMDGFELTRKLREQNSSLP 1032
Cdd:PRK09390    1 SDKGVVHVVDDDEAMRDSLAFLLDSAGFEVrlfESAQAFLDALPGLR---FGCVVTDVRMPGIDGIELLRRLKARGSPLP 77

                  .
gi 16130302  1033 I 1033
Cdd:PRK09390   78 V 78
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
836-937 4.62e-05

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 46.54  E-value: 4.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  836 LLSNALKFTteGAVKITTSLGHIDDNhavIKMTIMDSGSGLSQEeqqqlfkrysqtsagrQQTGSGLGLMICKELIKNMQ 915
Cdd:COG4585  170 ALTNALKHA--GATRVTVTLEVDDGE---LTLTVRDDGVGFDPE----------------AAPGGGLGLRGMRERAEALG 228
                         90       100
                 ....*....|....*....|..
gi 16130302  916 GDLSLESHPGIGTTFTITIPVE 937
Cdd:COG4585  229 GTLTIGSAPGGGTRVRATLPLA 250
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
825-934 6.19e-05

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 43.99  E-value: 6.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  825 DPQAFKQVLSNLLSNALKfTTEGAVKIT------------------TSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFK 886
Cdd:cd16938    8 DERRVFQVLLHMLGNLLK-MRNGGGNITfrvfleggsedrsdrdwgPWRPSMSDESVEIRFEVEINDSGSPSIESASMRN 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 16130302  887 rYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITI 934
Cdd:cd16938   87 -SLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
308-506 7.49e-05

Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and related proteins; the type 2 periplasmic-binding protein fold; This family comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270222 [Multi-domain]  Cd Length: 228  Bit Score: 45.36  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  308 ENPYsPPYSMTDENGSVRGVMGDILNIITLQTGLNFSPITVShnihagtqlspggWD-IIPG-------AIYS-----ED 374
Cdd:cd01001    9 EGDY-PPFNFLDADGKLVGFDIDLANALCKRMKVKCEIVTQP-------------WDgLIPAlkagkydAIIAsmsitDK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  375 RENNVLFAEAFITTPYVFVMQK----APDSEQTLKkGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELD 450
Cdd:cd01001   75 RRQQIDFTDPYYRTPSRFVARKdspiTDTTPAKLK-GKRVGVQAGTTHEAYLRDRFPEADLVEYDTPEEAYKDLAAGRLD 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130302  451 ALVA---------TQLNSR---YMIDHYYPNELYHFliPGVpnaslSFAFPRGEPELKDIINKALNAI 506
Cdd:cd01001  154 AVFGdkvalsewlKKTKSGgccKFVGPAVPDPKYFG--DGV-----GIAVRKDDDALRAKLDKALAAL 214
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
312-503 8.03e-05

Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein fold; This subfamily comprises of the periplasmic-binding protein component of ABC transporter specific for cysteine and its closely related proteins. The cysteine-binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270412 [Multi-domain]  Cd Length: 229  Bit Score: 45.42  E-value: 8.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  312 SPPYSMTDENGSVRGVMGDILNIIT-----LQTGLNFSPITVSHNIhagTQLSPGGWDIIPgAIYS--EDRENNVLFAea 384
Cdd:cd13694   18 KPPFGYVDENGKFQGFDIDLAKQIAkdlfgSGVKVEFVLVEAANRV---PYLTSGKVDLIL-ANFTvtPERAEVVDFA-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  385 fitTPYVFVMQK--APDSEQTLK----KGMKVAIPYYYELHSQLKEMYPEVEWIQVDNASAAFHKVKEGELDALVATQL- 457
Cdd:cd13694   92 ---NPYMKVALGvvSPKDSNITSvaqlDGKTLLVNKGTTAEKYFTKNHPEIKLLKYDQNAEAFQALKDGRADAYAHDNIl 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16130302  458 ---------NSRYMIDHYYPNElyhFLIPGVpnaslsfafPRGEPELKDIINKAL 503
Cdd:cd13694  169 vlawaksnpGFKVGIKNLGDTD---FIAPGV---------QKGNKELLEFINAEI 211
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
960-1040 8.27e-05

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 43.16  E-value: 8.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDE-ATDGVQALHKVSMQHYDLLITDVNMP-NMDGFELTRKLREqNSSLPIWGLT 1037
Cdd:cd17534    2 KILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIRE-KFDIPVIFLT 80

                 ...
gi 16130302 1038 ANA 1040
Cdd:cd17534   81 AYS 83
PRK10337 PRK10337
sensor protein QseC; Provisional
689-927 8.41e-05

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 46.57  E-value: 8.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   689 TETRDLINALEVEKNKAIKATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEI 768
Cdd:PRK10337  214 SEVRPLVEALNQLFARTHAMMVRERRFTSDAAHELRSPLAALKVQTEVAQLSDDDPQARKKALLQLHAGIDRATRLVDQL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   769 LDVDKIESGNYQLQPQWVDIPTLVQNTC--HSFGAIAASKSIALSCSSTFPEHylvKIDPQAFKQVLSNLLSNALKFTTE 846
Cdd:PRK10337  294 LTLSRLDSLDNLQDVAEIPLEDLLQSAVmdIYHTAQQAGIDVRLTLNAHPVIR---TGQPLLLSLLVRNLLDNAIRYSPQ 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   847 G-AVKITTSLGHIddnhavikmTIMDSGSGLSQEEQQQLFKRYSQtSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPG 925
Cdd:PRK10337  371 GsVVDVTLNARNF---------TVRDNGPGVTPEALARIGERFYR-PPGQEATGSGLGLSIVRRIAKLHGMNVSFGNAPE 440

                  ..
gi 16130302   926 IG 927
Cdd:PRK10337  441 GG 442
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
962-1051 1.25e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 44.50  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   962 LIADDHPTNRLLLKRQLNLLGYDV-DEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANa 1040
Cdd:PRK09958    4 IIIDDHPLAIAAIRNLLIKNDIEIlAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAK- 82
                          90
                  ....*....|.
gi 16130302  1041 qaNEREKGLSC 1051
Cdd:PRK09958   83 --NDHFYGKHC 91
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
837-935 1.27e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 41.77  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  837 LSNALKFTteGAVKITTSLGHIDDNhavIKMTIMDSGSGlsqeeqqqlfkRYSQTSAGrqqtGSGLGLMICKELIKNMQG 916
Cdd:cd16917    9 LTNALKHA--GASRVRVTLSYTADE---LTLTVVDDGVG-----------FDGPAPPG----GGGFGLLGMRERAELLGG 68
                         90
                 ....*....|....*....
gi 16130302  917 DLSLESHPGIGTTFTITIP 935
Cdd:cd16917   69 TLTIGSRPGGGTRVTARLP 87
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
982-1038 1.38e-04

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 42.57  E-value: 1.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130302  982 GYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTA 1038
Cdd:cd17572   22 GYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITA 78
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
961-1040 1.75e-04

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 45.63  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHS 85
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
988-1043 2.68e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 44.49  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302   988 ATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTANAQAN 1043
Cdd:PRK12555   32 ATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAE-RPCPILIVTSLTERN 86
PBP2_SMa0082_like cd01072
The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic ...
313-522 2.75e-04

The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Sinorhizobium meliloti and its related proteins. The putative SMa0082-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270233 [Multi-domain]  Cd Length: 238  Bit Score: 43.79  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  313 PPYSMTDENGSVRGVMGDILNII--TLQTGLNFSPITVSHNIhagTQLSPGGWDI-IPGAIYSEDRENNVLFAEafittP 389
Cdd:cd01072   24 PPFGFVDASMQPQGYDVDVAKLLakDLGVKLELVPVTGANRI---PYLQTGKVDMlIASLGITPERAKVVDFSQ-----P 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  390 Y-VFVMQKAPDSEQTLK-----KGMKVAIPYYYELHSQLKEMYPEVEWIQ-VDNASAAFHKVKEGELDAL-----VATQL 457
Cdd:cd01072   96 YaAFYLGVYGPKDAKVKspadlKGKTVGVTRGSTQDIALTKAAPKGATIKrFDDDASTIQALLSGQVDAIatgnaIAAQI 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130302  458 NSRYMIDHYypnELYHFLIpgvpNASLSFAFPRGEPELKDIINKALNAIPPSEVLR-LTEKWIKMP 522
Cdd:cd01072  176 AKANPDKKY---ELKFVLR----TSPNGIGVRKGEPELLKWVNTFIAKNKANGELNaLSQKWFGTP 234
PBP2_AatB_like cd00996
Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong ...
313-506 3.08e-04

Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong to the type 2 periplasmic binding fold protein superfamily; This subfamily includes periplasmic binding domain of ATP-binding cassette transporter-like systems that serve as initial receptors in the ABC transport of amino acids and their derivatives in eubacteria. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The Abp proteins belong to the PBPI superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270217 [Multi-domain]  Cd Length: 227  Bit Score: 43.72  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  313 PPYSMTDENGSVRGVMGDILNIITLQTGLN--FSPITVSHNIhagTQLSPGGWDII-PGAIYSEDRENNVLFAEAFITTP 389
Cdd:cd00996   15 APMGFRDENGEIVGFDIDLAKEVAKRLGVEveFQPIDWDMKE---TELNSGNIDLIwNGLTITDERKKKVAFSKPYLENR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  390 YVFVMQKapDSEQTLKKGMK-------------VAIPYYYELHSQLKEMYpevewiQVDNASAAFHKVKEGELDALVATQ 456
Cdd:cd00996   92 QIIVVKK--DSPINSKADLKgktvgvqsgssgeDALNADPNLLKKNKEVK------LYDDNNDAFMDLEAGRIDAVVVDE 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16130302  457 LNSRYMIDHYyPNELYHFLIPGVPNASLSFAFPRGEPELKDIINKALNAI 506
Cdd:cd00996  164 VYARYYIKKK-PLDDYKILDESFGSEEYGVGFRKEDTELKEKINKALDEM 212
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
961-1077 3.16e-04

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 41.56  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGY--DVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTA 1038
Cdd:cd19931    1 VLLIDDHPLLRKGIKQLIELDPDftVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16130302 1039 NAQANEREKGLSCGMNLCLFKPLTLDVLkthLSQLHQVA 1077
Cdd:cd19931   81 SDAEDDVVTALRAGADGYLLKDMEPEDL---LEALKQAA 116
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
871-935 3.91e-04

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 42.57  E-value: 3.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130302  871 DSGSGLSQEEQQQL-----FKRYSQTS--AGRqqtgsGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16916  112 DEAATLSDDEVLNLifapgFSTAEQVTdvSGR-----GVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
960-1070 4.43e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 43.25  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLReQNSSLPIWGLTAN 1039
Cdd:PRK10529    3 NVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR-QWSAIPVIVLSAR 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 16130302  1040 AQANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
Cdd:PRK10529   82 SEESDKIAALDAGADDYLSKPFGIGELQARL 112
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
836-935 5.15e-04

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 41.94  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  836 LLSNALKFTTEGA---------VKITTSLGhidDNHAVIKmtIMDSGSGLSQEEQQQLFKrYSQTSAGRQQT-------- 898
Cdd:cd16929   51 LLKNAMRATVESHgddsddlppIKVTVAKG---DEDLTIK--ISDRGGGIPREDLARLFS-YMYSTAPQPSLddfsdlis 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 16130302  899 --------GSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:cd16929  125 gtqpsplaGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
960-1037 5.59e-04

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 40.89  E-value: 5.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130302  960 SILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLT 1037
Cdd:cd17563    2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLT 79
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
985-1024 6.40e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 43.60  E-value: 6.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 16130302   985 VDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKL 1024
Cdd:PRK00742   32 VGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKI 71
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
950-1060 7.42e-04

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 42.75  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   950 EQPITlPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLReQNS 1029
Cdd:PRK10710    3 ELPID-ENTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR-RFS 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 16130302  1030 SLPIWGLTANAQANEREKGLSCGMNLCLFKP 1060
Cdd:PRK10710   81 DIPIVMVTAKIEEIDRLLGLEIGADDYICKP 111
PBP2_Arg_3 cd13622
Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding ...
302-427 7.65e-04

Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding fold; This subgroup is similar to the HisJ-like family that comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270340 [Multi-domain]  Cd Length: 222  Bit Score: 42.29  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  302 PNLKVLENPYSPPYSMTDENGSVRGVMGDILNII--TLQTGLNFSPITVSHNIHAgtqLSPGGWDIIPGAIY-SEDRENN 378
Cdd:cd13622    2 KPLIVGVGKFNPPFEMQGTNNELFGFDIDLMNEIckRIQRTCQYKPMRFDDLLAA---LNNGKVDVAISSISiTPERSKN 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 16130302  379 VLFAEAFITTPYVFVMQKAPDSEQTLK--KGMKVAIPYYYELHSQLKEMYP 427
Cdd:cd13622   79 FIFSLPYLLSYSQFLTNKDNNISSFLEdlKGKRIGILKGTIYKDYLLQMFV 129
PRK10859 PRK10859
membrane-bound lytic murein transglycosylase MltF;
357-519 8.71e-04

membrane-bound lytic murein transglycosylase MltF;


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 43.32  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   357 QLSPGGWDII-PGAIYSEDRENNVLFAEafittPYVFVMQK--------APDSEQTLKKGmKVAIP----YYYELhSQLK 423
Cdd:PRK10859   96 ALDKGKADLAaAGLTYTPERLKQFRFGP-----PYYSVSQQlvyrkgqpRPRSLGDLKGG-TLTVAagssHVETL-QELK 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   424 EMYPEVEWIQVDNASAA--FHKVKEGELDALVAT----QLNSRymidhYYPNELYHFLIpgVPNASLSFAFPRGE-PELK 496
Cdd:PRK10859  169 KKYPELSWEESDDKDSEelLEQVAEGKIDYTIADsveiSLNQR-----YHPELAVAFDL--TDEQPVAWALPPSGdDSLY 241
                         170       180
                  ....*....|....*....|....
gi 16130302   497 DIINKALNAIPPSEVL-RLTEKWI 519
Cdd:PRK10859  242 AALLDFFNQIKEDGTLaRLEEKYF 265
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
889-936 9.55e-04

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 43.25  E-value: 9.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 16130302  889 SQTSaGRqqtgsGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPV 936
Cdd:COG0643  377 TDLS-GR-----GVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
961-1061 1.33e-03

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 39.99  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNrLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLR--EQNSSLPIwglTA 1038
Cdd:cd17539    1 VLLVDDRPSS-AERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRslERTRQLPI---LA 76
                         90       100
                 ....*....|....*....|....*.
gi 16130302 1039 NAQANERE---KGLSCGMNLCLFKPL 1061
Cdd:cd17539   77 VADPGDRGrliRALEIGVNDYLVRPI 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
961-1060 1.46e-03

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 39.31  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALH--KVSMQHYDLLITDVNMPNMDGFELTRKLREQNS--SLPIWGL 1036
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDvlEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKIckNIPVIMM 80
                         90       100
                 ....*....|....*....|....
gi 16130302 1037 TANAQANEREKGLSCGMNLCLFKP 1060
Cdd:cd17582   81 SSQDSVGVVFKCLSKGAADYLVKP 104
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
298-519 2.21e-03

Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic binding protein fold; This subfamily represents the periplasmic-binding protein component of ABC transporter specific for carboxylic amino acids, including GtlI from Escherichia coli. The aspartate-glutamate binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270406 [Multi-domain]  Cd Length: 238  Bit Score: 41.08  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  298 IKQHPNLKVLENPYSPPYSMTDENGSVRGVMGDILNIITLQTG---------LNFSPITVSHNIHAgtqLSPGGWDIIPG 368
Cdd:cd13688    4 IRRTGTLTLGYREDSVPFSYLDDNGKPVGYSVDLCNAIADALKkklalpdlkVRYVPVTPQDRIPA---LTSGTIDLECG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  369 A-IYSEDRENNVLFAEAFITTPYVFVMQKA--PDSEQTLkKGMKVA-------IPYyyeLHSQLKEMYPEVEWIQVDNAS 438
Cdd:cd13688   81 AtTNTLERRKLVDFSIPIFVAGTRLLVRKDsgLNSLEDL-AGKTVGvtagtttEDA---LRTVNPLAGLQASVVPVKDHA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  439 AAFHKVKEGELDALVATQLNSRYMIDHY-YPNELyhFLIPGVPN-ASLSFAFPRGEPELKDIINKAL-NAIPPSEVLRLT 515
Cdd:cd13688  157 EGFAALETGKADAFAGDDILLAGLAARSkNPDDL--ALIPRPLSyEPYGLMLRKDDPDFRLLVDRALaQLYQSGEIEKLY 234

                 ....
gi 16130302  516 EKWI 519
Cdd:cd13688  235 DKWF 238
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
961-1062 2.94e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 40.86  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQ--NSSLPIWGLTA 1038
Cdd:PRK10161    5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKREsmTRDIPVVMLTA 84
                          90       100
                  ....*....|....*....|....
gi 16130302  1039 NAQANEREKGLSCGMNLCLFKPLT 1062
Cdd:PRK10161   85 RGEEEDRVRGLETGADDYITKPFS 108
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
961-1066 3.23e-03

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 38.42  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302  961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQnSSLPIWGLTANA 1040
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI-SNVPIIFISSRD 79
                         90       100
                 ....*....|....*....|....*.
gi 16130302 1041 QANEREKGLSCGMNLCLFKPLTLDVL 1066
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVL 105
PRK13560 PRK13560
hypothetical protein; Provisional
832-936 3.72e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 41.58  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   832 VLSNLLSNALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSqeeqQQLFKRYSQTsagrqqtgsgLGLMICKELI 911
Cdd:PRK13560  715 IISELLSNALKHAFPDGAAGNIKVEIREQGDGMVNLCVADDGIGLP----AGFDFRAAET----------LGLQLVCALV 780
                          90       100
                  ....*....|....*....|....*
gi 16130302   912 KNMQGDLSLESHPgiGTTFTITIPV 936
Cdd:PRK13560  781 KQLDGEIALDSRG--GARFNIRFPM 803
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
955-1044 6.69e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 39.45  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   955 LPEKLS--ILIADDHP-TNRLLLKRQLNLLGYDV-DEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSS 1030
Cdd:PRK10403    1 MPEATPfqVLIVDDHPlMRRGVRQLLELDPGFEVvAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVT 80
                          90
                  ....*....|....
gi 16130302  1031 LPIWGLTANAQANE 1044
Cdd:PRK10403   81 AQIIILTVSDASSD 94
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
824-935 9.39e-03

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 40.20  E-value: 9.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130302   824 IDPQAFKQVLSNLLSNALKF---TTEGAVKITTSLGhiDDNHAVIkMTIMDSGSGLSQEEQQQLFKRYSQTSAgRQQTGS 900
Cdd:PRK15053  428 LDSTEFAAIVGNLLDNAFEAslrSDEGNKIVELFLS--DEGDDVV-IEVADQGCGVPESLRDKIFEQGVSTRA-DEPGEH 503
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16130302   901 GLGLMICKELIKNMQGDLSLESHPGIGTTFTITIP 935
Cdd:PRK15053  504 GIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH