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Conserved domains on  [gi|697052506|ref|WP_033145112|]
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MULTISPECIES: sulfonate ABC transporter substrate-binding protein [Enterobacter]

Protein Classification

sulfonate ABC transporter substrate-binding protein( domain architecture ID 10013830)

sulfonate ABC transporter substrate-binding protein SsuA serves as initial receptor in the ABC transport of aliphatic sulfonates; is involved in the assimilation of sulfur

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11553 PRK11553
alkanesulfonate transporter substrate-binding subunit; Provisional
2-315 0e+00

alkanesulfonate transporter substrate-binding subunit; Provisional


:

Pssm-ID: 236929  Cd Length: 314  Bit Score: 602.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   2 FKTLTRIGLAGLMALSSLAHAAEAAPESLRIGYQKGSVSMVLAKSHQLLEKRFPDTKFSWVEFPAGPQMLEALNVGSIDL 81
Cdd:PRK11553   1 MRNIIKLALAGLLSVSTLAVAAESSPEALRIGYQKGSIGLVLAKSHQLLEKRFPQTKISWVEFPAGPQMLEALNVGSIDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  82 GSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQP 161
Cdd:PRK11553  81 GSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVAENSPIKTVADLKGHKVAFQKGSSSHNLLLRALRKAGLKFTDIQP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 162 VYLTPADARAAFQQKNVDAWAIWDPYYSAALLQGGVRVLKDGTTLKQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALT 241
Cdd:PRK11553 161 TYLTPADARAAFQQGNVDAWAIWDPYYSAALLQGGVRVLKDGTDLNQTGSFYLAARPYAEKNGAFIQQVLATLTEADALT 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052506 242 QTQRQESIALLAKTMGLPEPVIASYLNHRPPTTITPVDAHVAALQQQTADLFYQNHLVPKQVTIRERIWQPAGK 315
Cdd:PRK11553 241 RSQREQSIALLAKTMGLPAAVIASYLDHRPPTTIKPLSAEVAAAQQQTADLFYENRLVPKKVDIRQRVWQPTQL 314
 
Name Accession Description Interval E-value
PRK11553 PRK11553
alkanesulfonate transporter substrate-binding subunit; Provisional
2-315 0e+00

alkanesulfonate transporter substrate-binding subunit; Provisional


Pssm-ID: 236929  Cd Length: 314  Bit Score: 602.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   2 FKTLTRIGLAGLMALSSLAHAAEAAPESLRIGYQKGSVSMVLAKSHQLLEKRFPDTKFSWVEFPAGPQMLEALNVGSIDL 81
Cdd:PRK11553   1 MRNIIKLALAGLLSVSTLAVAAESSPEALRIGYQKGSIGLVLAKSHQLLEKRFPQTKISWVEFPAGPQMLEALNVGSIDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  82 GSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQP 161
Cdd:PRK11553  81 GSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVAENSPIKTVADLKGHKVAFQKGSSSHNLLLRALRKAGLKFTDIQP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 162 VYLTPADARAAFQQKNVDAWAIWDPYYSAALLQGGVRVLKDGTTLKQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALT 241
Cdd:PRK11553 161 TYLTPADARAAFQQGNVDAWAIWDPYYSAALLQGGVRVLKDGTDLNQTGSFYLAARPYAEKNGAFIQQVLATLTEADALT 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052506 242 QTQRQESIALLAKTMGLPEPVIASYLNHRPPTTITPVDAHVAALQQQTADLFYQNHLVPKQVTIRERIWQPAGK 315
Cdd:PRK11553 241 RSQREQSIALLAKTMGLPAAVIASYLDHRPPTTIKPLSAEVAAAQQQTADLFYENRLVPKKVDIRQRVWQPTQL 314
PBP2_SsuA cd13557
Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic ...
30-303 2.74e-140

Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the sulfonate binding domains SsuA found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins belong to the PBPII 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: 270275  Cd Length: 275  Bit Score: 397.43  E-value: 2.74e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSvSMVLAKSHQLLEKRF--PDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPP 107
Cdd:cd13557    2 LRIGYQKGG-TLVLLKARGELEKRLkpLGVKVTWSEFPAGPQLLEALNVGSIDFGSTGDTPPIFAQAAGAPLVYVAVEPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 108 KPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPY 187
Cdd:cd13557   81 TPKGEAILVPKDSPIKTVADLKGKKIAFQKGSSAHYLLVKALEKAGLTLDDIEPVYLSPADARAAFEQGQVDAWAIWDPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 188 YSAALLQGGVRVLKDGTTLKQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALTQTQRQESIALLAKTMGLPePVIASYL 267
Cdd:cd13557  161 LAAAELTGGARVLADGEGLVNNRSFYLAARDFAKDNPEAIQIVLEELNKAGEWANTNRDEAAKLLAESLGID-AVVLELA 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 697052506 268 NHRPPTTITPVDAHVAALQQQTADLFYQNHLVPKQV 303
Cdd:cd13557  240 VARRTYGIIPIDDEIIAAQQAIADTFYDLGLIPKKV 275
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
30-310 3.25e-87

ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins. [Transport and binding proteins, Other]


Pssm-ID: 130789 [Multi-domain]  Cd Length: 288  Bit Score: 263.07  E-value: 3.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   30 LRIGYQK-GSVSMVLAKSHQLLEKRFPDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPk 108
Cdd:TIGR01728   1 VRIGYQKnGHSALALAKEKGLLEKELGKTKVEWVEFPAGPPALEALGAGSLDFGYIGPGPALFAYAAGADIKAVGLVSD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  109 PKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPYY 188
Cdd:TIGR01728  80 NKATAIVVIKGSPIRTVADLKGKRIAVPKGGSGHDLLLRALLKAGLSGDDVTILYLGPSDARAAFAAGQVDAWAIWEPWG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  189 SAALLQGGVRVLKDGTT--LKQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALTQTQRQESIALLAKTMGLPEPVIASY 266
Cdd:TIGR01728 160 SALVEEGGARVLANGEGigLPGQPGFLVVRREFAEAHPEQVQRVLKVLVKARKWAEENPEESAKILAKELGLSQAVVEET 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 697052506  267 LNHRPPTTITPVDAHVAALQQQTADLFYQNHLVPKQVTIRERIW 310
Cdd:TIGR01728 240 VLNRRFLRVEVISDAVVDALQAMADFFYAAGLLKKKPDLKDAVD 283
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
10-303 3.67e-67

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 212.17  E-value: 3.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  10 LAGLMALSSLAHAAEAAPESLRIGYQK--GSVSMVLAKSHQLLEKRfpDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDI 87
Cdd:COG0715    4 LAALALAACSAAAAAAEKVTLRLGWLPntDHAPLYVAKEKGYFKKE--GLDVELVEFAGGAAALEALAAGQADFGVAGAP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  88 PPIFAQAAGADLVYVGVEPPKPkAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPA 167
Cdd:COG0715   82 PALAARAKGAPVKAVAALSQSG-GNALVVRKDSGIKSLADLKGKKVAVPGGSTSHYLLRALLAKAGLDPKDVEIVNLPPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 168 DARAAFQQKNVDAWAIWDPYYSAALLQGGVRVLKDGTTL--KQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALTQTQR 245
Cdd:COG0715  161 DAVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLvpGYPGDVLVASEDFLEENPEAVKAFLRALLKAWAWAAANP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 697052506 246 QESIALLAKTMGLPEPVIASYLNHRPPTTiTPVDAHVAALQQQTADLFYQNHLVPKQV 303
Cdd:COG0715  241 DEAAAILAKATGLDPEVLAAALEGDLRLD-PPLGAPDPARLQRVADFLVELGLLPKDV 297
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
29-232 1.48e-29

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 112.42  E-value: 1.48e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506    29 SLRIGYQKGSVSMVLAKSHQLLE-------KRFPD---TKFSWVEFpAGPQMLEALNVGSIDLGSTG-DIPPIFAQAAGA 97
Cdd:smart00062   1 TLRVGTNGDYPPFSFADEDGELTgfdvdlaKAIAKelgLKVEFVEV-SFDSLLTALKSGKIDVVAAGmTITPERAKQVDF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506    98 DLVYVGVEPpkpkaeVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDiqpvylTPADARAAFQQKN 177
Cdd:smart00062  80 SDPYYRSGQ------VILVRKDSPIKSLEDLKGKKVAVVAGTTAEELLKKLYPEAKIVSYD------SNAEALAALKAGR 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 697052506   178 VDAWAIWDPYYSAALLQGGVRVLKDGTTLK-QTGSFYLAARPYAEKNGAFIQGVLD 232
Cdd:smart00062 148 ADAAVADAPLLAALVKQHGLPELKIVPDPLdTPEGYAIAVRKGDPELLDKINKALK 203
NMT1 pfam09084
NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed ...
64-188 1.57e-10

NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed to be required for the biosynthesis of the pyrimidine moiety of thiamine.3]. They are regulated by thiamine. The protein adopts a fold related to the periplasmic binding protein (PBP) family. Both pyridoxal-5'-phosphate (PLP) and an iron atom are bound to the protein suggesting numerous residues of the active site necessary for HMP-P biosynthesis. The yeast protein is a dimer and, although exceptionally using PLP as a substrate, has notable similarities with enzymes dependent on this molecule as a cofactor.


Pssm-ID: 430398 [Multi-domain]  Cd Length: 216  Bit Score: 59.93  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   64 FPAGP-QMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGV---EPPkpkaEVILVPENSDIKSVADLKGHKVAFQKGS 139
Cdd:pfam09084  27 EPADPsDATQLVASGKADFGVSYQESVLLARAKGLPVVSVAAliqHPL----SGVISLKDSGIKSPKDLKGKRIGYSGSP 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 697052506  140 SSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWaiWDPYY 188
Cdd:pfam09084 103 FEEALLKALLKKDGGDPDDVTIVNVGGMNLFPALLTGKVDAA--IGGYY 149
 
Name Accession Description Interval E-value
PRK11553 PRK11553
alkanesulfonate transporter substrate-binding subunit; Provisional
2-315 0e+00

alkanesulfonate transporter substrate-binding subunit; Provisional


Pssm-ID: 236929  Cd Length: 314  Bit Score: 602.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   2 FKTLTRIGLAGLMALSSLAHAAEAAPESLRIGYQKGSVSMVLAKSHQLLEKRFPDTKFSWVEFPAGPQMLEALNVGSIDL 81
Cdd:PRK11553   1 MRNIIKLALAGLLSVSTLAVAAESSPEALRIGYQKGSIGLVLAKSHQLLEKRFPQTKISWVEFPAGPQMLEALNVGSIDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  82 GSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQP 161
Cdd:PRK11553  81 GSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVAENSPIKTVADLKGHKVAFQKGSSSHNLLLRALRKAGLKFTDIQP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 162 VYLTPADARAAFQQKNVDAWAIWDPYYSAALLQGGVRVLKDGTTLKQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALT 241
Cdd:PRK11553 161 TYLTPADARAAFQQGNVDAWAIWDPYYSAALLQGGVRVLKDGTDLNQTGSFYLAARPYAEKNGAFIQQVLATLTEADALT 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697052506 242 QTQRQESIALLAKTMGLPEPVIASYLNHRPPTTITPVDAHVAALQQQTADLFYQNHLVPKQVTIRERIWQPAGK 315
Cdd:PRK11553 241 RSQREQSIALLAKTMGLPAAVIASYLDHRPPTTIKPLSAEVAAAQQQTADLFYENRLVPKKVDIRQRVWQPTQL 314
PBP2_SsuA cd13557
Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic ...
30-303 2.74e-140

Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the sulfonate binding domains SsuA found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins belong to the PBPII 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: 270275  Cd Length: 275  Bit Score: 397.43  E-value: 2.74e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSvSMVLAKSHQLLEKRF--PDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPP 107
Cdd:cd13557    2 LRIGYQKGG-TLVLLKARGELEKRLkpLGVKVTWSEFPAGPQLLEALNVGSIDFGSTGDTPPIFAQAAGAPLVYVAVEPP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 108 KPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPY 187
Cdd:cd13557   81 TPKGEAILVPKDSPIKTVADLKGKKIAFQKGSSAHYLLVKALEKAGLTLDDIEPVYLSPADARAAFEQGQVDAWAIWDPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 188 YSAALLQGGVRVLKDGTTLKQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALTQTQRQESIALLAKTMGLPePVIASYL 267
Cdd:cd13557  161 LAAAELTGGARVLADGEGLVNNRSFYLAARDFAKDNPEAIQIVLEELNKAGEWANTNRDEAAKLLAESLGID-AVVLELA 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 697052506 268 NHRPPTTITPVDAHVAALQQQTADLFYQNHLVPKQV 303
Cdd:cd13557  240 VARRTYGIIPIDDEIIAAQQAIADTFYDLGLIPKKV 275
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
30-310 3.25e-87

ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins. [Transport and binding proteins, Other]


Pssm-ID: 130789 [Multi-domain]  Cd Length: 288  Bit Score: 263.07  E-value: 3.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   30 LRIGYQK-GSVSMVLAKSHQLLEKRFPDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPk 108
Cdd:TIGR01728   1 VRIGYQKnGHSALALAKEKGLLEKELGKTKVEWVEFPAGPPALEALGAGSLDFGYIGPGPALFAYAAGADIKAVGLVSD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  109 PKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPYY 188
Cdd:TIGR01728  80 NKATAIVVIKGSPIRTVADLKGKRIAVPKGGSGHDLLLRALLKAGLSGDDVTILYLGPSDARAAFAAGQVDAWAIWEPWG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  189 SAALLQGGVRVLKDGTT--LKQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALTQTQRQESIALLAKTMGLPEPVIASY 266
Cdd:TIGR01728 160 SALVEEGGARVLANGEGigLPGQPGFLVVRREFAEAHPEQVQRVLKVLVKARKWAEENPEESAKILAKELGLSQAVVEET 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 697052506  267 LNHRPPTTITPVDAHVAALQQQTADLFYQNHLVPKQVTIRERIW 310
Cdd:TIGR01728 240 VLNRRFLRVEVISDAVVDALQAMADFFYAAGLLKKKPDLKDAVD 283
PBP2_SsuA_like_2 cd13558
Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding ...
30-295 6.80e-74

Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins 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: 270276  Cd Length: 267  Bit Score: 228.32  E-value: 6.80e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSVSMVLAKSHQLlekrfPDT--KFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPP 107
Cdd:cd13558    2 LRVGDQKGGLRALLEAAGEL-----DGLpyKIEWAEFQGGAPLLEALRAGALDIGGAGDTPPLFAAAAGAPIKIVAALRG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 108 KPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPY 187
Cdd:cd13558   77 DVNGQALLVPKDSPIRSVADLKGKRVAYVRGSISHYLLLKALEKAGLSPSDVELVFLTPADALAAFASGQVDAWATWGPY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 188 YSAALLQGGVRVLKDGTTLKQTGSFYLAARP---YAEKNGAfIQGVLDTFTQADALTQTQRQESIALLAKTMGLPEPVIA 264
Cdd:cd13558  157 VARAERRGGARVLVTGEGLILGLSFVVAARPallDPAKRAA-IADFLARLARAQAWANAHPDEWAKAYAAETGLPPEVAA 235
                        250       260       270
                 ....*....|....*....|....*....|.
gi 697052506 265 SYLNHRPPTTItPVDAHVAALQQQTADLFYQ 295
Cdd:cd13558  236 AIFARRSAPVV-PIDAQVIASQQQTADTFHE 265
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
10-303 3.67e-67

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 212.17  E-value: 3.67e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  10 LAGLMALSSLAHAAEAAPESLRIGYQK--GSVSMVLAKSHQLLEKRfpDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDI 87
Cdd:COG0715    4 LAALALAACSAAAAAAEKVTLRLGWLPntDHAPLYVAKEKGYFKKE--GLDVELVEFAGGAAALEALAAGQADFGVAGAP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  88 PPIFAQAAGADLVYVGVEPPKPkAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPA 167
Cdd:COG0715   82 PALAARAKGAPVKAVAALSQSG-GNALVVRKDSGIKSLADLKGKKVAVPGGSTSHYLLRALLAKAGLDPKDVEIVNLPPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 168 DARAAFQQKNVDAWAIWDPYYSAALLQGGVRVLKDGTTL--KQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALTQTQR 245
Cdd:COG0715  161 DAVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLvpGYPGDVLVASEDFLEENPEAVKAFLRALLKAWAWAAANP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 697052506 246 QESIALLAKTMGLPEPVIASYLNHRPPTTiTPVDAHVAALQQQTADLFYQNHLVPKQV 303
Cdd:COG0715  241 DEAAAILAKATGLDPEVLAAALEGDLRLD-PPLGAPDPARLQRVADFLVELGLLPKDV 297
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
30-237 1.04e-64

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. 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 domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins 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: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 202.90  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSVSM--VLAKSHQLLEKRFPDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPP 107
Cdd:cd01008    2 VRIGYQAGPLAGplIVAKEKGLFEKEKEGIDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLAAAGGVPVVLIAALSR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 108 KPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPY 187
Cdd:cd01008   82 SPNGNGIVVRKDSGITSLADLKGKKIAVTKGTTGHFLLLKALAKAGLSVDDVELVNLGPADAAAALASGDVDAWVTWEPF 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 697052506 188 YSAALLQGGVRVLKDGTTLKQTGSFYLAAR-PYAEKNGAFIQGVLDTFTQA 237
Cdd:cd01008  162 LSLAEKGGDARIIVDGGGLPYTDPSVLVARrDFVEENPEAVKALLKALVEA 212
PBP2_SsuA_like_5 cd13562
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
30-237 6.63e-50

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes sulfonate binding domains found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins 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: 270280 [Multi-domain]  Cd Length: 215  Bit Score: 165.37  E-value: 6.63e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQK--GSVSMVLAKSHQLLEKRFP----DTKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVG 103
Cdd:cd13562    2 IRIGFQPipPYAPILVAKQKGWLEEELKkagaDVGVKWSQFSAGPPVNEAFAAGELDVGLLGDTPAIIGRAAGQDTRIVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 104 VEPPKPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAI 183
Cdd:cd13562   82 LASTGPKALALVVRKDSAIKSVKDLKGKKVATTKGSYVHHLLVLVLQEAGLTIDDVEFINMQQADMNTALTNGDIDAAVI 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 697052506 184 WDPYYSAALLQGGVRVLKDGTTLKQTGSFYLAARPYAEKNGAFIQGVLDTFTQA 237
Cdd:cd13562  162 WEPLITKLLSDGVVRVLRDGTGIKDGLNVIVARGPLIEQNPEVVKALLKAYQRG 215
PBP2_SsuA_like_1 cd13556
Substrate binding domain of putative sulfonate binding protein, a member of the type 2 ...
30-285 1.96e-41

Substrate binding domain of putative sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins 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: 270274  Cd Length: 265  Bit Score: 144.92  E-value: 1.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGS-VSMVLaKSHQLLEKRF-PD-TKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADL--VYVGv 104
Cdd:cd13556    2 LRLDYAYYNpVSLVL-KKFGWLEKEFqKDgVKVTWVLSQGSNKALEFLNSGSVDFGSTAGLAALLAKANGNPIktVYVY- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 105 epPKPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIW 184
Cdd:cd13556   80 --SRPEWTALVVRKDSPIRSVADLKGKKVAVTKGTDPYIFLLRALNTAGLSKNDIEIVNLQHADGRTALEKGDVDAWAGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 185 DPYYSAALLQGGVRVLKDGTTLkQTGSFYLAARPYAEKNGAFIQGVLDTFTQADALTQTQRQESIALLAKTMGLPEPVIA 264
Cdd:cd13556  158 DPFMAQTELENGSRLFYRNPDF-NTYGVLNVREDFAKRHPDAVRRVLKVYEKARKWAITHPDELAQILASESKLSLAVAK 236
                        250       260
                 ....*....|....*....|.
gi 697052506 265 SYLNHRPPTTITPVDAHVAAL 285
Cdd:cd13556  237 LQLSRTDFSQPIPGPAQIAVL 257
TauA COG4521
ABC-type taurine transport system, periplasmic component [Inorganic ion transport and ...
4-265 4.07e-37

ABC-type taurine transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443595 [Multi-domain]  Cd Length: 332  Bit Score: 135.38  E-value: 4.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   4 TLTRIGLAGLMALSS--LAHAAEAAPESLRIGYQKGSVSMVLAKSHQLLEKRFpDTKFSWVEFPAGPQMLEALNVGSIDL 81
Cdd:COG4521    2 KFKRLLLLAALALAGcaLAAAAAAAAKEVTIGYQTIPNPELVAKADGALEKAL-GAKVNWRKFDSGADVITALASGDVDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  82 GSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQP 161
Cdd:COG4521   81 GSIGSSPFAAALSRGLPIEVIWIADVIGDAEALVVRNGSGITSPKDLKGKKIAVPFGSTSHYSLLAALKHAGIDPSDVTI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 162 VYLTPADARAAFQQKNVDAWAIWDPyysaALLqggvRVLKDGTTL----------KQTGSFYLAARPYAEKNGAFIQGVL 231
Cdd:COG4521  161 LNMQPPEIAAAWQRGDIDAAYVWDP----ALS----ELKKSGKVLitsaelakwgAPTFDVWVVRKDFAEENPDFVAAFL 232
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 697052506 232 DTFTQADALTQT--QRQESIALLAKTMGLPEPVIAS 265
Cdd:COG4521  233 KVLADAVADYRAdpAAWPAAKAIAKLLGADPEDAPA 268
PBP2_taurine cd13560
Taurine-binding periplasmic protein; the type 2 periplasmic binding protein fold; This ...
30-223 5.22e-31

Taurine-binding periplasmic protein; the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins 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: 270278 [Multi-domain]  Cd Length: 218  Bit Score: 115.86  E-value: 5.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSVSMVLAKSHQLLEKRFPDtKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPKP 109
Cdd:cd13560    2 IRIGYQTVPNPQLVAKADGLLEKALGV-KVNWRKFDSGADVNAAMASGSIDIGLLGSPPAAVAIAAGLPIEVIWIADVIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 110 KAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPyyS 189
Cdd:cd13560   81 DAEALVVRKGSGIKSLKDLAGKKVAVPFGSTAHYSLLAALKHAGVDPGKVKILDMQPPEIVAAWQRGDIDAAYVWEP--A 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 697052506 190 AALLQGGVRVLKDGTTLKQ----TGSFYLAARPYAEKN 223
Cdd:cd13560  159 LSQLKKNGKVLLSSKDLAKkgilTFDVWVVRKDFAEKY 196
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
29-232 1.48e-29

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 112.42  E-value: 1.48e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506    29 SLRIGYQKGSVSMVLAKSHQLLE-------KRFPD---TKFSWVEFpAGPQMLEALNVGSIDLGSTG-DIPPIFAQAAGA 97
Cdd:smart00062   1 TLRVGTNGDYPPFSFADEDGELTgfdvdlaKAIAKelgLKVEFVEV-SFDSLLTALKSGKIDVVAAGmTITPERAKQVDF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506    98 DLVYVGVEPpkpkaeVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDiqpvylTPADARAAFQQKN 177
Cdd:smart00062  80 SDPYYRSGQ------VILVRKDSPIKSLEDLKGKKVAVVAGTTAEELLKKLYPEAKIVSYD------SNAEALAALKAGR 147
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 697052506   178 VDAWAIWDPYYSAALLQGGVRVLKDGTTLK-QTGSFYLAARPYAEKNGAFIQGVLD 232
Cdd:smart00062 148 ADAAVADAPLLAALVKQHGLPELKIVPDPLdTPEGYAIAVRKGDPELLDKINKALK 203
PBP2_sulfate_ester_like cd13555
Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold; This ...
58-264 3.48e-29

Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins 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: 270273  Cd Length: 268  Bit Score: 112.43  E-value: 3.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  58 KFSWVEFP-AGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVIlVPENSDIKSVADLKGHKVAFQ 136
Cdd:cd13555   40 KVEWVFFKgAGPAVNEAFANGQIDFAVYGDLPAIIGRAAGLDTKLLLSSGSGNNAYLV-VPPDSTIKSVKDLKGKKVAVQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 137 KGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPYYsAALLQGGVRVL---KDGTTLKQTGSFY 213
Cdd:cd13555  119 KGTAWQLTFLRILAKNGLSEKDFKIVNLDAQDAQAALASGDVDAAFTGYEAL-KLEDQGAGKIIwstKDKPEDWTTQSGV 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 697052506 214 LAARPYAEKNGAFIQGVLDTFTQADA-LTQTQRQESIALLAKTMGLPEPVIA 264
Cdd:cd13555  198 WARTDFIKENPDVVQRIVTALVKAARwVSQEENRDEYIQLWSRSGTPEELIK 249
PBP2_SsuA_like_6 cd13563
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ...
29-237 3.71e-29

Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins 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: 270281 [Multi-domain]  Cd Length: 208  Bit Score: 110.79  E-value: 3.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  29 SLRIGYQK--GSVSMVLAKSHQLLEKRFPDtkFSWVEFPAGPQMLEALNVGSIDLGST--GDIPPIFAQaaGADLVYVGV 104
Cdd:cd13563    1 PLKIGISTwpGYGPWYLADEKGFFKKEGLD--VELVWFESYSDSMAALASGQIDAAATtlDDALAMAAK--GVPVKIVLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 105 EPPKPKAEVILVPenSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIW 184
Cdd:cd13563   77 LDNSNGADGIVAK--PGIKSIADLKGKTVAVEEGSVSHFLLLNALEKAGLTEKDVKIVNMTAGDAGAAFIAGQVDAAVTW 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 697052506 185 DPYYSAALLQGGVRVLKDGTTLKQTGSFYLAARP-YAEKNGAFIQGVLDTFTQA 237
Cdd:cd13563  155 EPWLSNALKRGKGKVLVSSADTPGLIPDVLVVREdFIKKNPEAVKAVVKAWFDA 208
PBP2_SsuA_like_3 cd13559
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
30-264 1.43e-28

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins 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: 270277  Cd Length: 258  Bit Score: 110.59  E-value: 1.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSVSMV----LAKSHQLLEKRFP------DTKF--SWVEFPAGPQMLEALNVGSIDLGSTGDIPPI-----FA 92
Cdd:cd13559    2 VAIGTQDTTINTAtgglLIRELGLLEKYLPelgkykDVEYeiEWQDFTSGAPLTNEMVAGKLDIGAMGDFPGLlngvkFQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  93 QAAGADLVYVGVEP--PKPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGL-KFTDIQPVYLTPADA 169
Cdd:cd13559   82 TSAGYRSVFIAFLGgsPDGSGNAIVVPKDSPVNSLDDLKGKTVSVPFGSSAHGMLLRALDRAGLnPDTDVTIINQAPEVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 170 RAAFQQKNVDAWAIWDPYYSAALLQGGVRVLKDGTtlkQTGSFYL----AARPYAEKNGAFIQGVLDTFTQADALTQTQR 245
Cdd:cd13559  162 GSALQANKIDAHADFVPFPELFPHRGIARKLYDGS---QTKVPTFhgivVDRDFAEKHPEVVVAYLRALIEAHRLIREEP 238
                        250
                 ....*....|....*....
gi 697052506 246 QESIALLAKTMGLPEPVIA 264
Cdd:cd13559  239 EAYSELIEKVTGIEAEVVY 257
PBP2_SsuA_like_4 cd13561
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
30-237 4.19e-25

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA proteins 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: 270279 [Multi-domain]  Cd Length: 212  Bit Score: 100.14  E-value: 4.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQK---GSVSMVLAKSHQLLEKRFPDTKFSWveFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEP 106
Cdd:cd13561    2 IRIGYLPalaVAGPIFIAKEKGLFAKHGLDPDFIE--FTSGPPLVAALGSGSLDVGYTGPVAFNLPASGQAKVVLINNLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 107 pKPKAEVIlVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDP 186
Cdd:cd13561   80 -NATASLI-VRADSGIASIADLKGKKIGTPSGTTADVALDLALRKAGLSEKDVQIVNMDPAEIVTAFTSGSVDAAALWAP 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 697052506 187 YYSAALLQG-GVRVLKDGTTLKQTGSF---YLAARPYAEKNGAFIQGVLDTFTQA 237
Cdd:cd13561  158 NTATIKEKVpGAVELADNSDFGPDAAVpgaWVARNKYAEENPEELKKFLAALAEA 212
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
29-200 5.66e-25

Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). 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 domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins 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: 270271 [Multi-domain]  Cd Length: 212  Bit Score: 99.96  E-value: 5.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  29 SLRIGYQK--GSVSMVLAKSHQLLEKrfPDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDI-PPIFAQAAGADLVYVGVE 105
Cdd:cd13553    1 TLRIGYLPitDHAPLLVAKEKGFFEK--EGLDVELVKFPSWADLRDALAAGELDAAHVLAPmPAAATYGKGAPIKVVAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 106 ppkpkAE---VILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLR-ALQEAGLKFT-DIQPVYLTPADARAAFQQKNVDA 180
Cdd:cd13553   79 -----HRngsAIVVSKDSGIKSVADLKGKTIAVPFPGSTHDVLLRyWLAAAGLDPGkDVEIVVLPPPDMVAALAAGQIDA 153
                        170       180
                 ....*....|....*....|
gi 697052506 181 WAIWDPYYSAALLQGGVRVL 200
Cdd:cd13553  154 YCVGEPWNARAVAEGVGRVL 173
PBP2_DszB cd13554
Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 ...
30-257 4.25e-20

Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes DszB, which converts 2'-hydroxybiphenyl-2-sulfinate to 2-hydroxybiphenyl and sulfinate at the rate-limiting step of the microbial dibenzothiophene desulfurization pathway. The overall fold of DszB is highly similar to those of periplasmic substrate-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. 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 domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The DszB protein belongs 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: 270272 [Multi-domain]  Cd Length: 246  Bit Score: 87.57  E-value: 4.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSVSMVLAKSHQLLEKRFPDTKfsWVEF-PAGPQMLEALNVGSIDLGSTGDIPPIFAQA--AGADLVYVGVEP 106
Cdd:cd13554    3 LRYSNCPVPNALLTAEESGYLDAAGIDLE--VVAGtPTGTVDFTYDQGIPADVVFSGAIPPLLAEGlrAPGRTRLIGITP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 107 PKPKAEVILVPENSDIKSVADLKGHKVAFQKGSSSHN----LLLRALQEAGLKfTDIQPVYLTPADARAAFQQKNVDAWA 182
Cdd:cd13554   81 LDLGRQGLFVRADSPITSAADLEGKRIGMSAGAIRGSwlarALLHNLEIGGLD-VEIVPIDSPGRGQAAALDSGDIDALA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052506 183 IWDPYYSAALLQGGVRVLKDGTTLK--QTGSFYLAARPYAEKNGAFIQGVLDTFTQADALTQTQRQESIALLAKTMG 257
Cdd:cd13554  160 SWLPWATTLQATGGARPLVDLGLVEgnSYYSTWTVRSDFIEQNPEAVKALVEALVRAGDWIQAHPEAVVIIHAAEIG 236
PBP2_ThiY_THI5_like_1 cd13652
Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 ...
62-203 1.64e-19

Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 periplasmic binding protein fold; This subfamily is phylogenetically similar to ThiY, which is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they 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. The ThiY/THI5 proteins 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: 270370 [Multi-domain]  Cd Length: 217  Bit Score: 85.13  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  62 VEFPAGPQMLEALNVGSIDLGSTGDIPPIF-AQAAGADLVYV---GVEPPKPKAEVILVPENSDIKSVADLKGHKVAFQK 137
Cdd:cd13652   36 TRFASGAEILAALASGQVDVAGSSPGASLLgALARGADLKIVaegLGTTPGYGPFAIVVRADSGITSPADLVGKKIAVST 115
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052506 138 GSSSHNLLLRA-LQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPYYSAALLQGGVRVLKDG 203
Cdd:cd13652  116 LTNILEYTTNAyLKKNGLDPDKVEFVEVAFPQMVPALENGNVDAAVLAEPFLSRARSSGAKVVASDY 182
Imp COG2358
TRAP-type uncharacterized transport system, periplasmic component [General function prediction ...
22-200 3.16e-16

TRAP-type uncharacterized transport system, periplasmic component [General function prediction only];


Pssm-ID: 441925 [Multi-domain]  Cd Length: 303  Bit Score: 77.58  E-value: 3.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  22 AAEAAPESLRIG-YQKGSVSMVLAKS-HQLLEKRFPDTKFSWVEFPAGPQMLEALNVGSIDLGstgdippiFAQAAGADL 99
Cdd:COG2358    6 AAAAAPQFLTIGtGGTGGTYYPIGGAiAKVVNKELPGIRVTVQSTGGSVENLRLLRAGEADLA--------IVQSDVAYD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 100 VYVGVEP--PKPKAEV------------ILVPENSDIKSVADLKGHKVAF-QKGSSSHNLLLRALQEAGLKFTDIQPVYL 164
Cdd:COG2358   78 AYNGTGPfeGGPLDNLralaslypepvhLVVRADSGIKSLADLKGKRVSVgPPGSGTEVTAERLLEAAGLTYDDVKVEYL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 697052506 165 TPADARAAFQQKNVDAWAIWDPYYSAALLQ----GGVRVL 200
Cdd:COG2358  158 GYGEAADALKDGQIDAAFFVAGLPTGAVTElaatTDIRLL 197
PBP2_TAXI_TRAP cd13520
Substrate binding domain of TAXI proteins of the tripartite ATP-independent periplasmic ...
71-216 2.07e-14

Substrate binding domain of TAXI proteins of the tripartite ATP-independent periplasmic transporters; the type 2 periplasmic binding protein fold; This group includes Thermus thermophilus GluBP (TtGluBP) of TAXI-TRAP family and closely related proteins. TRAP transporters are ubiquitous in prokaryotes, but absent from eukaryotes. They are comprised of an SBP (substrate-binding protein) of the DctP or TAXI families and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function. The substrate-binding domain of TAXI proteins 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 tworeceptor cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270238 [Multi-domain]  Cd Length: 285  Bit Score: 72.27  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  71 LEALNVGSIDLGstgdippiFAQAAGADLVYVGVEPPKPKAEV--------------ILVPENSDIKSVADLKGHKVAF- 135
Cdd:cd13520   45 LRLLESGEADFG--------LAQSDVAYDAYNGTGPFEGKPIDnlravaslypeylhLVVRKDSGIKSIADLKGKRVAVg 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 136 QKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAwAIW-----DPYYSAALLQGGVRVL----KDGTTL 206
Cdd:cd13520  117 PPGSGTELTARRLLEAYGLTDDDVKAEYLGLSDAADALKDGQIDA-FFWvgglpASAITELAATRDIRLLpiddEEIAKL 195
                        170
                 ....*....|
gi 697052506 207 KQTGSFYLAA 216
Cdd:cd13520  196 LAEYPYYVPA 205
tauA PRK11480
taurine transporter substrate binding subunit; Provisional
13-292 1.01e-11

taurine transporter substrate binding subunit; Provisional


Pssm-ID: 183158  Cd Length: 320  Bit Score: 64.62  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  13 LMALSSLAHAAEAApeSLRIGYQKGSVSMVLAKSHQLLEKRfPDTKFSWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFA 92
Cdd:PRK11480  10 LAALAFIAFQAQAV--NVTVAYQTSAEPAKVAQADNTFAKE-SGATVDWRKFDSGASIVRALASGDVQIGNLGSSPLAVA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  93 QAAGADLVYVGVEPPKPKAEVILVPENsdIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAA 172
Cdd:PRK11480  87 ASQQVPIEVFLLASKLGNSEALVVKKT--ISKPEDLIGKRIAVPFISTTHYSLLAALKHWGIKPGQVEIVNLQPPAIIAA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 173 FQQKNVDAWAIWDPYYSAALLQGgvRVLKDGTTLKQTGS----FYLAARPYAEKN----GAFIQGVLDtfTQADALTQT- 243
Cdd:PRK11480 165 WQRGDIDGAYVWAPAVNALEKDG--KVLTDSEQVGQWGAptldVWVVRKDFAEKHpevvKAFAKSAID--AQQPYIANPd 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 697052506 244 ---QRQESIALLAKTMGLPEPVIASYLnhRPPTTITPvdahvaalQQQTADL 292
Cdd:PRK11480 241 awlKQPENISKLARLSGVPEGDVPGLV--KGNTYLTP--------QQQTAEL 282
NMT1 pfam09084
NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed ...
64-188 1.57e-10

NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed to be required for the biosynthesis of the pyrimidine moiety of thiamine.3]. They are regulated by thiamine. The protein adopts a fold related to the periplasmic binding protein (PBP) family. Both pyridoxal-5'-phosphate (PLP) and an iron atom are bound to the protein suggesting numerous residues of the active site necessary for HMP-P biosynthesis. The yeast protein is a dimer and, although exceptionally using PLP as a substrate, has notable similarities with enzymes dependent on this molecule as a cofactor.


Pssm-ID: 430398 [Multi-domain]  Cd Length: 216  Bit Score: 59.93  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   64 FPAGP-QMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGV---EPPkpkaEVILVPENSDIKSVADLKGHKVAFQKGS 139
Cdd:pfam09084  27 EPADPsDATQLVASGKADFGVSYQESVLLARAKGLPVVSVAAliqHPL----SGVISLKDSGIKSPKDLKGKRIGYSGSP 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 697052506  140 SSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDAWaiWDPYY 188
Cdd:pfam09084 103 FEEALLKALLKKDGGDPDDVTIVNVGGMNLFPALLTGKVDAA--IGGYY 149
PBP2_Cae31940 cd13649
Substrate binding domain of an uncharacterized protein similar to ABC-type transporter for ...
63-233 5.56e-10

Substrate binding domain of an uncharacterized protein similar to ABC-type transporter for thiamin biosynthetic pathway intermediates; a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplamic-binding protein Cae31940 which is phylogenetically similar to the ThiY/THI5 family. ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, They 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. The ThiY/THI5 proteins 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: 270367  Cd Length: 223  Bit Score: 58.31  E-value: 5.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  63 EFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVPENS-DIKSVADLKGHKVAFQK-GSS 140
Cdd:cd13649   37 DFGGGSKALQALVGGSVDVVTGAYEHTIRMQARGQDIKAFCELGRFPGICIGVRKDLAgDIKTIADLKGQNVGVTApGSS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 141 SHNLLLRALQEAGLKFTDIQPVYLTP-ADARAAFQQKNVDAWAIWDPYYSAALLQGGVRVLKDGTTLKQT----GSFYLA 215
Cdd:cd13649  117 TSLLLNYALIKNGLKPDDVSIIGVGGgASAVAAIKKGQIDAISNLDPVITRLEVDGDITLLLDTRTEKGTrelfGGTNPA 196
                        170
                 ....*....|....*...
gi 697052506 216 ARPYAEKngAFIQGVLDT 233
Cdd:cd13649  197 ATLYVQQ--AFIDANPVT 212
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
58-201 2.61e-09

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: 56.53  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  58 KFSWVEFPAgPQMLEALNVGSIDLGSTGdippIFAQAAGADLVYVgVEPPKPKAEVILVPE-NSDIKSVADLKGHKVAFQ 136
Cdd:COG0834   39 KVEFVPVPW-DRLIPALQSGKVDLIIAG----MTITPEREKQVDF-SDPYYTSGQVLLVRKdNSGIKSLADLKGKTVGVQ 112
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697052506 137 KGSSSHNLLLRALQEAGLKFTDiqpvylTPADARAAFQQKNVDAWAIWDPYYSAALLQGGVRVLK 201
Cdd:COG0834  113 AGTTYEEYLKKLGPNAEIVEFD------SYAEALQALASGRVDAVVTDEPVAAYLLAKNPGDDLK 171
PBP2_BztA cd13692
Substrate bindng domain of ABC glutamate/glutamine/aspartate/asparagine transporter; the type ...
114-182 7.20e-09

Substrate bindng domain of ABC glutamate/glutamine/aspartate/asparagine transporter; the type 2 periplasmic binding protein fold; BztA is the periplamic-binding protein component of ABC transporter specific for carboxylic amino acids, glutamine and asparagine. The BZtA 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: 270410 [Multi-domain]  Cd Length: 236  Bit Score: 55.33  E-value: 7.20e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052506 114 ILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIqpVYLTPADARAAFQQKNVDAWA 182
Cdd:cd13692  103 FLVRKDSGITSAKDLDGATICVQAGTTTETNLADYFKARGLKFTPV--PFDSQDEARAAYFSGECDAYT 169
3A0109s03R TIGR01098
phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are ...
1-184 7.84e-09

phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are a varied class of phosphorus-containing organic compound in which a direct C-P bond is found, rather than a C-O-P linkage of the phosphorus through an oxygen atom. They may be toxic but also may be used as sources of phosphorus and energy by various bacteria. Phosphonate utilization systems typically are encoded in 14 or more genes, including a three gene ABC transporter. This family includes the periplasmic binding protein component of ABC transporters for phosphonates as well as other, related binding components for closely related substances such as phosphate and phosphite. A number of members of this family are found in genomic contexts with components of selenium metabolic processes suggestive of a role in selenate or other selenium-compound transport. A subset of this model in which nearly all members exhibit genomic context with elements of phosphonate metabolism, particularly the C-P lyase system (GenProp0232) has been built (TIGR03431) as an equivalog. Nevertheless, there are members of this subfamily (TIGR01098) which show up sporadically on a phylogenetic tree that also show phosphonate context and are most likely competent to transport phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 273442 [Multi-domain]  Cd Length: 254  Bit Score: 55.43  E-value: 7.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506    1 MFKTLTRIGLAGLMALSSL----AHAAEAAPESLRIGYQKGSVSMVLAKSHQ----LLEKRFPdTKFSWVEFPAGPQMLE 72
Cdd:TIGR01098   1 MKRLLALLAALLGASLAAAcskkAAEAAAVPKELNFGILPGENASNLTRRWEpladYLEKKLG-IKVQLFVATDYSAVIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   73 ALNVGSIDLGSTGdiPPIFAQA-----AGADLVYVGVEPPKPKAE-VILVPENSDIKSVADLKGHKVAFQ-KGSSSHNLL 145
Cdd:TIGR01098  80 AMRFGRVDIAWFG--PSSYVLAhyranAEVFALTAVSTDGSPGYYsVIIVKADSPIKSLKDLKGKTFAFGdPASTSGYLV 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 697052506  146 LRA--LQEAGLK--FTDIQPVYLTPADARAAF-QQKNVDAWAIW 184
Cdd:TIGR01098 158 PRYqlKKEGGLDadGFFSEVVFSGSHDASALAvANGKVDAATNN 201
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
68-200 1.07e-08

ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 54.93  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  68 PQMLEALNVGSIDLGSTGdiPPIFAQA---AGADLVYVGVEPPKPKAE-VILVPENSDIKSVADLKGHKVAF-QKGSSSH 142
Cdd:COG3221   38 AALIEALRAGQVDLAFLG--PLPYVLArdrAGAEPLATPVRDGSPGYRsVIIVRADSPIKSLEDLKGKRFAFgDPDSTSG 115
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052506 143 NLLLRA-LQEAGLKFTD--IQPVYL-TPADARAAFQQKNVDAWAIWDPYYSAALLQG----GVRVL 200
Cdd:COG3221  116 YLVPRAlLAEAGLDPERdfSEVVFSgSHDAVILAVANGQADAGAVDSGVLERLVEEGpdadQLRVI 181
PBP2_TtGluBP cd13567
Substrate binding domain of Thermus thermophilus GluBP (TtGluBP) of TAXI family of the ...
114-180 1.52e-08

Substrate binding domain of Thermus thermophilus GluBP (TtGluBP) of TAXI family of the tripartite ATP-independent periplasmic transporters; contains the type 2 periplasmic binding protein fold; This subgroup includes TtGluBP of TAXI-TRAP family and closely related proteins. TRAP transporters are comprised of an SBP (substrate-binding protein) and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function.


Pssm-ID: 270285 [Multi-domain]  Cd Length: 284  Bit Score: 54.91  E-value: 1.52e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052506 114 ILVPENSDIKSVADLKGHKVAFQK-GSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAAFQQKNVDA 180
Cdd:cd13567   94 IVVRADSGIKTVADLKGKRVSVGApGSGTEVNARQILEAAGLTYDDIKVVYLSFAEAAEALKDGQIDA 161
PBP2_ThiY_THI5_like cd13564
Substrate binding domain of ABC-type transporter for thiamin biosynthetic pathway ...
64-237 1.56e-08

Substrate binding domain of ABC-type transporter for thiamin biosynthetic pathway intermediates and similar proteins; the type 2 periplasmic binding protein fold; ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they 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. The ThiY/THI5 proteins 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: 270282 [Multi-domain]  Cd Length: 214  Bit Score: 54.05  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  64 FPAGP-QMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPKPKAEViLVPENSDIKSVADLKGHKVAFQKGSSSH 142
Cdd:cd13564   37 TPTGGsDIVQLVASGQFDFGLSAVTHTLVAQSKGVPVKAVASAIRKPFSGV-TVLKDSPIKSPADLKGKKVGYNGLKNIN 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 143 NLLLRALQE-AGLKFTDIQPVYLTPADARAAFQQKNVDAWAIWDPYYSAALLQGG-VRVLKDGTTLKQ--TGSFYLAARP 218
Cdd:cd13564  116 ETAVRASVRkAGGDPEDVKFVEVGFDQMPAALDSGQIDAAQGTEPALATLKSQGGdIIASPLVDVAPGdlTVAMLITNTA 195
                        170
                 ....*....|....*....
gi 697052506 219 YAEKNGAfiqgVLDTFTQA 237
Cdd:cd13564  196 YVQQNPE----VVKAFQAA 210
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
68-200 2.13e-08

ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake.


Pssm-ID: 432911 [Multi-domain]  Cd Length: 243  Bit Score: 54.19  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   68 PQMLEALNVGSIDLGSTGDIPPIFA-QAAGADLVYVGVEPP-KPKAE-VILVPENSDIKSVADLKGHKVAF-QKGSSSHN 143
Cdd:pfam12974  40 AAVVEALRAGQVDIAYFGPLAYVQAvDRAGAEPLATPVEPDgSAGYRsVIIVRKDSPIQSLEDLKGKTVAFgDPSSTSGY 119
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052506  144 LLLRAL--QEAGLKF-TDIQPVYLTPAD-ARAAFQQKNVDAWA----IWDPYYSA-ALLQGGVRVL 200
Cdd:pfam12974 120 LVPLALlfAEAGLDPeDDFKPVFSGSHDaVALAVLNGDADAGAvnseVLERLVAEgPIDRDQLRVI 185
PBP2_AA_hypothetical cd13623
Substrate-binding domain of putative amino-acid transport system; the type 2 periplasmic ...
62-204 2.15e-08

Substrate-binding domain of putative amino-acid transport system; the type 2 periplasmic binding protein fold; This putative amino acid-binding protein 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: 270341 [Multi-domain]  Cd Length: 220  Bit Score: 53.83  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  62 VEFPAGPQMLEALNVGSIDLGSTGDIPpifAQAAGADL--VYVGVEppkpkaEVILVPENSDIKSVADL--KGHKVAFQK 137
Cdd:cd13623   48 VVFPAAGAVVDAASDGEWDVAFLAIDP---ARAETIDFtpPYVEIE------GTYLVRADSPIRSVEDVdrPGVKIAVGK 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052506 138 GSSSHNLLLRALQEAGLKftdiqpVYLTPADARAAFQQKNVDAWA-IWDPYYSAALLQGGVRVLkDGT 204
Cdd:cd13623  119 GSAYDLFLTRELQHAELV------RAPTSDEAIALFKAGEIDVAAgVRQQLEAMAKQHPGSRVL-DGR 179
PBP2_PhnD_like cd01071
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ...
25-197 2.20e-08

Substrate binding domain of phosphonate uptake system-like, a member of the type 2 periplasmic-binding fold superfamily; This family includes alkylphosphonate binding domain PhnD. These domains are found in PhnD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate. PhnD belongs 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. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270232 [Multi-domain]  Cd Length: 253  Bit Score: 54.19  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  25 AAPESLRIGYQKGSVSMVLAKSHQ----LLEKRFPDTkfswVEFPAGPQ---MLEALNVGSIDLGSTGDIPPIFA-QAAG 96
Cdd:cd01071    1 AAPKELRFGLVPAEDADELKKEFEpladYLEEELGVP----VELVVATSyaaVVEAMRNGKVDIAWLGPASYVLAhDRAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  97 ADLVYVGVEPPKPKAE-VILVPENSDIKSVADLKGHKVAFQ-KGSSSHNLLLRA-LQEAGL--KFTDIQPVYL-TPADAR 170
Cdd:cd01071   77 AEALATEVRDGSPGYYsVIIVRKDSPIKSLEDLKGKTVAFVdPSSTSGYLFPRAmLKDAGIdpPDFFFEVVFAgSHDSAL 156
                        170       180
                 ....*....|....*....|....*..
gi 697052506 171 AAFQQKNVDAWAIWDPYYSAALLQGGV 197
Cdd:cd01071  157 LAVANGDVDAAATYDSTLERAAAAGPI 183
PBP2_Ca3427_like cd13637
The conserved hypothetical protein Ca3427 exhibits the type 2 periplasmic-binding protein fold; ...
47-267 2.56e-08

The conserved hypothetical protein Ca3427 exhibits the type 2 periplasmic-binding protein fold; This group includes the Ca3427 protein from candida albicans, which is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8, and other related hypothetical proteins. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. Ca3427 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. 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: 270355  Cd Length: 273  Bit Score: 54.11  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  47 HQLLEKRFP---DTKFSWVEFPAGP-QMLEALNVGSIDL--GST-GDIPPIFAQAAGADLVYVGVEPPKPKAevILVPEN 119
Cdd:cd13637   16 HLAIEEGFFaehGINVEWVDFPGGTgAMIKALRNGEIDIaiGLTeGFVADIAKGGNPYKIVGTYVASPLNWA--IHTGAN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 120 SDIKSVADLKGHKVAF-QKGSSSH---NLLlrALQEaGLKFTDIQPVYLTPAD-ARAAFQQKNVDAWaIWD-----PYYs 189
Cdd:cd13637   94 SDYNSIEDLKGTKIGIsRIGSGSHlmaYVL--ALQQ-GWDTEDLKFEVLNNFDgLRDAVNDGKADAF-MWEhfttkPYV- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 190 aallqggvrvlkDGTTLKQTG-------SFYLAARP-YAEKNGAFIQGVLDTFTQADALTQTQRQESIALLAKTMGLPEP 261
Cdd:cd13637  169 ------------DSGEFKRIGeiptpwpSFVIAASDeLLEENPEALKAFLDALNQGIAYFKAHPEEAVEYIAKRYDYKEE 236

                 ....*.
gi 697052506 262 VIASYL 267
Cdd:cd13637  237 DAREWL 242
TRAP_TAXI TIGR02122
TRAP transporter solute receptor, TAXI family; This family is one of at least three major ...
1-180 3.24e-08

TRAP transporter solute receptor, TAXI family; This family is one of at least three major families of extracytoplasmic solute receptor (ESR) for TRAP (Tripartite ATP-independent Periplasmic Transporter) transporters. The others are the DctP (TIGR00787) and SmoM (pfam03480) families. These transporters are secondary (driven by an ion gradient) but composed of three polypeptides, although in some species the 4-TM and 12-TM integral membrane proteins are fused. Substrates for this transporter family are not fully characterized but, besides C4 dicarboxylates, may include mannitol and other compounds. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273982 [Multi-domain]  Cd Length: 320  Bit Score: 54.26  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506    1 MFKTLTRIGLAGLMALSSLAHAAEA--APESLRIGyqKGSVSMV-------LAkshQLLEKRFPDTKFSWVEFPAGPQML 71
Cdd:TIGR02122   1 MKKRLFLLGAALAIVGAALAACAGDggEPTFVTIG--TGGTGGVyypiggaIA---QLINKKSGKLRVRVQSTGGSVENV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   72 EALNVGSIDLGSTGDIPPIFAQAAgaDLVYVGVEPPK---------PKAEVILVPENSDIKSVADLKGHKVAFQKGSSSH 142
Cdd:TIGR02122  76 NLLEAGEADLAIVQSDVAYYAYEG--DGEFEFEGPVEklralaslyPEYIQIVVRKDSGIKTVADLKGKRVAVGAPGSGT 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 697052506  143 NLLLRA-LQEAGLKFTDI-QPVYLTPADARAAFQQKNVDA 180
Cdd:TIGR02122 154 ELNARAvLKAAGLTYDDVkKVEYLGYAEAADALKDGKIDA 193
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
113-218 5.25e-08

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: 52.68  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  113 VILVPENS---DIKSVADLKGHKVAFQKGSSSHNLllraLQEAGLKFTDIQpVYLTPADARAAFQQKNVDAWAIWDPYYS 189
Cdd:pfam00497  88 VILVRKKDsskSIKSLADLKGKTVGVQKGSTAEEL----LKNLKLPGAEIV-EYDDDAEALQALANGRVDAVVADSPVAA 162
                          90       100
                  ....*....|....*....|....*....
gi 697052506  190 AALLQGGVRVLKDGTTLKQTGSFYLAARP 218
Cdd:pfam00497 163 YLIKKNPGLNLVVVGEPLSPEPYGIAVRK 191
PBP2_TAXI_TRAP_like_1 cd13569
Substrate binding domain of putative TAXI proteins of the tripartite ATP-independent ...
48-180 2.06e-07

Substrate binding domain of putative TAXI proteins of the tripartite ATP-independent periplasmic transporters; the type 2 periplasmic binding protein fold; This subgroup includes uncharacterized periplasmic binding proteins that are related to Thermus thermophilus GluBP (TtGluBP) of TAXI-TRAP family. TRAP transporters are comprised of an SBP (substrate-binding protein) and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function.


Pssm-ID: 270287 [Multi-domain]  Cd Length: 283  Bit Score: 51.50  E-value: 2.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  48 QLLEKRFPDTKFSWVEFPAGPQMLEALNVGSIDLGstgdippiFAQAAGADLVYVGVEPPKPKAEV------------IL 115
Cdd:cd13569   22 EILSKAVPDVRATAEVTGASVENLRLVASGEADLG--------FALADAALDAYNGEGPFSGPVPLralarlypnylhLV 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052506 116 VPENSDIKSVADLKGHKVAF-QKGSSSHNLLLRALQEAGLK-FTDIQPVYLTPADARAAFQQKNVDA 180
Cdd:cd13569   94 VRADSGITSLEDLKGKRVSVgAPGSGTEVTAERLLEAAGLDpDKDVKRERLGLAESVAALKDGQIDA 160
PBP2_PnhD_2 cd13572
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
25-237 2.89e-07

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. 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: 270290 [Multi-domain]  Cd Length: 249  Bit Score: 50.77  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  25 AAPESLRIGYQKGSVSMVLAKSHQLLEKRFPDTKFSWVEFPAGPQ---MLEALNVGSIDLGSTGDIPPIFA-QAAGADLV 100
Cdd:cd13572    1 QAPETLKVGAIPDENPTTLIRLNDPLADYLEKELGVEVELVVVTDyaaMVEAMRNGQLDLAYFGGLTYVQArLKPGAEPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 101 YVGVEPPKPKAE-VILVPENSDIKSVADLKGHKVAF-QKGSSSHNLLLR-ALQEAGL--KFTDIQPVYLTPADARA-AFQ 174
Cdd:cd13572   81 AQLLRDGDPTFHsVFIANTDSGINSLADLKGKRFAFgDPASTSGHLMPRyFLLEAGVlpDGDFYRVGFSGAHDATAlAVA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052506 175 QKNVDAWAIWDPYYSAALLQGGVrvlkDGTTLK---QTGsfylaarPYAEKNGAFIQGVLDTFTQA 237
Cdd:cd13572  161 NGKVDAGALNEAIWESLVEEGKI----DGEKVKviwRTP-------PYPDYPWTVRPNLGPELKEK 215
OpuAC pfam04069
Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity ...
28-267 1.66e-06

Substrate binding domain of ABC-type glycine betaine transport system; Part of a high affinity multicomponent binding-protein-dependent transport system involved in bacterial osmoregulation. This domain is often fused to the permease component of the transporter complex. Family members are often integral membrane proteins or predicted to be attached to the membrane by a lipid anchor. Glycine betaine is involved in protection from high osmolarity environments for example in Bacillus subtilis. The family member OpuBC is closely related, and involved in choline transport. Choline is necessary for the biosynthesis of glycine betaine. L-carnitine is important for osmoregulation in Listeria monocytogenes. Family also contains proteins binding l-proline (ProX), histidine (HisX) and taurine (TauA).


Pssm-ID: 397954 [Multi-domain]  Cd Length: 257  Bit Score: 48.48  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   28 ESLRIGYQKGSVSMVLAK-SHQLLEKRfpDTKFSWVEFPAGPQMLEALNVGSIDL---GSTGDIPPIFAQAAGADLVYVG 103
Cdd:pfam04069   1 KTIVIGSKNWTEQEILANiAAQLLEAL--GYVVELVGLGSSAVLFAALASGDIDLypeEWTGTTYEAYKKAVEEKLGLLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  104 VEPPKPKA-EVILVP----ENSDIKSVADLKGHKVAF-----------QKGSSSHNLLLRALQEAGLKFTDIQPVYLTPA 167
Cdd:pfam04069  79 LGPLGAGNtYGLAVPkyvaEKPGIKSISDLAKPADDLelgfkgefigrPDGWGCMRSTEGLLKAYGLDKYELVEGSEAAM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  168 DA--RAAFQQKNVDAWAIWDPyySAALLQGGVRVLKDGTTLK-QTGSFYLAARP-YAEKNGAfIQGVLDTFTqadaLTQT 243
Cdd:pfam04069 159 DAliYAAYKRGEPDVVYAWTP--DWMIKKYDLVVLEDPKGLFpPAYNVVPVVRKgFAEKHPE-VAAFLNKLS----LDTE 231
                         250       260
                  ....*....|....*....|....
gi 697052506  244 QRQESIALLAKTMGLPEPVIASYL 267
Cdd:pfam04069 232 DLNELNAQVDVEGKDPEEVAKDWL 255
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
27-253 3.59e-06

NMT1-like family; This family is closely related to the pfam09084 family.


Pssm-ID: 463863  Cd Length: 254  Bit Score: 47.34  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506   27 PESLRIGYQK--GSVSMVLAKshqllEKRFP---DTKFSWVEFPAGPQMLEALNVGSIDLG--STGdippifaQAAGADL 99
Cdd:pfam13379   5 KTSLKLGFIPltDAAPLIVAA-----EKGFFakyGLTVELSKQASWAETRDALVAGELDAAhvLTP-------MPYLITL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  100 VYVGveppKPKAEVILVPENS-----------------DIKSVADLKGHKVAFQKG--------SSSHNLLLR-ALQEAG 153
Cdd:pfam13379  73 GIGG----AKVPMIVLASLNLngqaitlankyadkgvrDAAALKDLVGAYKASGKPfkfavtfpGSTHDLWLRyWLAAGG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  154 LK-FTDIQPVYLTPADARAAFQQKNVDAWAIWDPYYSAALLQG-GVRVLKDGTTLKQTGSFYLAAR-PYAEKN----GAF 226
Cdd:pfam13379 149 LDpDADVKLVVVPPPQMVANLRAGNIDGFCVGEPWNARAVAEGiGVTAATTGELWKDHPEKVLGVRaDWVDKNpnaaRAL 228
                         250       260
                  ....*....|....*....|....*..
gi 697052506  227 IQGVLDTFTQADALTQTqRQESIALLA 253
Cdd:pfam13379 229 VKALIEATRWLDAKPEN-RREAAKLLA 254
PBP2_AatB_like cd00996
Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong ...
113-180 6.46e-06

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: 46.42  E-value: 6.46e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052506 113 VILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRalqEAGLKFTDIQPV-YLTPADARAAFQQKNVDA 180
Cdd:cd00996   93 IIVVKKDSPINSKADLKGKTVGVQSGSSGEDALNA---DPNLLKKNKEVKlYDDNNDAFMDLEAGRIDA 158
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
112-196 8.53e-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: 46.22  E-value: 8.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 112 EVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLlralqEAGLKFTDIQPvYLTPADARAAFQQKNVDAwAIWDPYYSAA 191
Cdd:cd13696   96 MVVLTRKDSGIKSFDDLKGKTVGVVKGSTNEAAV-----RALLPDAKIQE-YDTSADAILALKQGQADA-MVEDNTVANY 168

                 ....*
gi 697052506 192 LLQGG 196
Cdd:cd13696  169 KASSG 173
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
111-218 9.08e-06

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: 46.09  E-value: 9.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 111 AEVILVPENSDIKS-VADLKGHKVAFQKGSSSHNLLLRALQEAGLKftdiqpVYLTPADARAAFQQKNVDAWAIwDPYYS 189
Cdd:cd13530   87 GQVLVVKKDSKITKtVADLKGKKVGVQAGTTGEDYAKKNLPNAEVV------TYDNYPEALQALKAGRIDAVIT-DAPVA 159
                         90       100
                 ....*....|....*....|....*....
gi 697052506 190 AALLQGGVRVLKDGTTLKQTGSFYLAARP 218
Cdd:cd13530  160 KYYVKKNGPDLKVVGEPLTPEPYGIAVRK 188
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
112-220 1.41e-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: 45.30  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 112 EVILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLK-FTDIQPVYLtpadaraAFQQKNVDAWAIwdpyySA 190
Cdd:cd13689   97 QKLLVKKGSGIKSLKDLAGKRVGAVKGSTSEAAIREKLPKASVVtFDDTAQAFL-------ALQQGKVDAITT-----DE 164
                         90       100       110
                 ....*....|....*....|....*....|
gi 697052506 191 ALLQGGVRVLKDGTTLKQTGsFYLAARPYA 220
Cdd:cd13689  165 TILAGLLAKAPDPGNYEILG-EALSYEPYG 193
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
55-198 1.42e-05

Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold; This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate 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: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 45.38  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  55 PDTKFSWVEFPAgPQMLEALNVGSIDL--GSTGdIPPIFAQAAGADLVYVGVEPPkpkaevILVPENSDIKSVADLKGHK 132
Cdd:cd01000   48 DPVKVKFVPVTS-ANRIPALQSGKVDLiiATMT-ITPERAKEVDFSVPYYADGQG------LLVRKDSKIKSLEDLKGKT 119
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 697052506 133 VAFQKGSSSHNLLLRALQEAglkftdiQPV-YLTPADARAAFQQKNVDAWAIwdpyySAALLQGGVR 198
Cdd:cd01000  120 ILVLQGSTAEAALRKAAPEA-------QLLeFDDYAEAFQALESGRVDAMAT-----DNSLLAGWAA 174
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
55-182 1.55e-05

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: 45.32  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  55 PDTKFSWVefPAGPQ-MLEALNVGSIDL--GSTGDI----------PPIFAqaAGAdlvyvgveppkpkaeVILVPENSD 121
Cdd:cd13688   52 PDLKVRYV--PVTPQdRIPALTSGTIDLecGATTNTlerrklvdfsIPIFV--AGT---------------RLLVRKDSG 112
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052506 122 IKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKfTDIQPvYLTPADARAAFQQKNVDAWA 182
Cdd:cd13688  113 LNSLEDLAGKTVGVTAGTTTEDALRTVNPLAGLQ-ASVVP-VKDHAEGFAALETGKADAFA 171
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
113-180 4.65e-05

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: 43.64  E-value: 4.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052506 113 VILVPENSD-IKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKftdiqpVYLTPADARAAFQQKNVDA 180
Cdd:cd13624   89 AIVVRKDSTiIKSLDDLKGKKVGVQIGTTGAEAAEKILKGAKVK------RFDTIPLAFLELKNGGVDA 151
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
113-210 4.68e-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: 43.80  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 113 VILVPE-NSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLK-FTDIQPVYLtpadaraAFQQKNVDAwAIWD-P--- 186
Cdd:cd00994   88 AVMVKAdNNSIKSIDDLAGKTVAVKTGTTSVDYLKENFPDAQLVeFPNIDNAYM-------ELETGRADA-VVHDtPnvl 159
                         90       100
                 ....*....|....*....|....
gi 697052506 187 YYSAALLQGGVRVLKDGTTLKQTG 210
Cdd:cd00994  160 YYAKTAGKGKVKVVGEPLTGEQYG 183
HemD COG1587
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ...
112-183 6.68e-05

Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III synthase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 441195  Cd Length: 229  Bit Score: 43.35  E-value: 6.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 112 EVILVPENSDIKSVADL----KGHKVAFQKGSSSHNLLLRALQEAGLKFTDI-----QPVYLTPADARAAFQQKNVDAWA 182
Cdd:COG1587  103 KVDLVPEGFTSEGLLELlqalAGKRVLIPRGDGGREDLAETLRAAGAEVDEVevyrtVPPDDLPEELLEALAAGEIDAVL 182

                 .
gi 697052506 183 I 183
Cdd:COG1587  183 F 183
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
118-180 1.03e-04

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: 42.96  E-value: 1.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052506 118 ENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDiqpvylTPADARAAFQQKNVDA 180
Cdd:cd13704   96 GSSIINSLEDLKGKKVAVQRGDIMHEYLKERGLGINLVLVD------SPEEALRLLASGKVDA 152
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
62-217 1.15e-04

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 42.56  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  62 VEFPAGPQMLEALNVGSIDLG-STGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVPENSDIKS---VADLKGHKVAF-Q 136
Cdd:cd00648   34 VPGSSIGTLIEALAAGDADVAvGPIAPALEAAADKLAPGGLYIVPELYVGGYVLVVRKGSSIKGllaVADLDGKRVGVgD 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 137 KGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARAA-FQQKNVDAWAIWDPYYSAALLQGGVRVLKDGTTLKQTGSFYLA 215
Cdd:cd00648  114 PGSTAVRQARLALGAYGLKKKDPEVVPVPGTSGALAaVANGAVDAAIVWVPAAERAQLGNVQLEVLPDDLGPLVTTFGVA 193

                 ..
gi 697052506 216 AR 217
Cdd:cd00648  194 VR 195
NMT1_3 pfam16868
NMT1-like family;
109-256 1.42e-04

NMT1-like family;


Pssm-ID: 435616 [Multi-domain]  Cd Length: 289  Bit Score: 42.62  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  109 PKAEVILVPENSDIKSVADLKGHKVAF-QKGSSSHNLLLRALQEAGLKFTDIQPV-YLTPADARAAFQQKNVDAWAIWDP 186
Cdd:pfam16868  90 PEPFQFVVSKDSGIGSIADLKGKRVSVgPPGSGTEGSTRAILGALGISYKDLSLLeYLGYGESADALKDGQLDGAFFPAG 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052506  187 YYSAALLQ----GGVRVLK-DGTTLKQTGSFYLAARPYAEKNGAFiQGVLDTFTQAD----ALTQTQRQESIALLAKTM 256
Cdd:pfam16868 170 PPVSAVTQlaasVDINLIGlDDEQLDKLLAEYPYWTPYIIPAGTY-PQDEDVPTIAVpnflVTRADLDEELVYLLTKAI 247
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
48-247 1.45e-04

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: 42.13  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  48 QLLEKRFPdTKFSWVEFPAGPQMLEALNVGSIDLgstgdIPPIFAQAAGADLVYVgvepPKPKAEVILV----PENSDIK 123
Cdd:cd01007   33 KLIAKKLG-LKFEYVPGDSWSELLEALKAGEIDL-----LSSVSKTPEREKYLLF----TKPYLSSPLVivtrKDAPFIN 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 124 SVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDiqpvylTPADARAAFQQKNVDAwAIwDPYYSAA--LLQGGVRVLK 201
Cdd:cd01007  103 SLSDLAGKRVAVVKGYALEELLRERYPNINLVEVD------STEEALEAVASGEADA-YI-GNLAVASylIQKYGLSNLK 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 697052506 202 DGTTLKQTGSFYLAARP-YAEkngafiqgVLDTFTQA-DALTQTQRQE 247
Cdd:cd01007  175 IAGLTDYPQDLSFAVRKdWPE--------LLSILNKAlASISPEERQA 214
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
114-207 2.47e-04

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: 41.57  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 114 ILVPENSDIKSVADLKGHKVAFQKGSSshnlllralQEAGLK--FTDIQPVYL-TPADARAAFQQKNVD----------A 180
Cdd:cd13694  101 VVSPKDSNITSVAQLDGKTLLVNKGTT---------AEKYFTknHPEIKLLKYdQNAEAFQALKDGRADayahdnilvlA 171
                         90       100       110
                 ....*....|....*....|....*....|...
gi 697052506 181 WAIWDPYYSAALLQGG------VRVLKDGTTLK 207
Cdd:cd13694  172 WAKSNPGFKVGIKNLGdtdfiaPGVQKGNKELL 204
PBP2_PnhD_4 cd13574
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
71-155 3.61e-04

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. 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: 270292 [Multi-domain]  Cd Length: 250  Bit Score: 41.53  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  71 LEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPP----KPKAEVILVPENSDIKSVADLKGHKVAF-QKGSSSHNLL 145
Cdd:cd13574   50 VDRLGSGKIDIAYLGPAPYVQAKDRRYGIKPLLALLEtdgkPTYNGVIVVRADSPIKSLADLAGKSFAFgDPLSTMGHLV 129
                         90
                 ....*....|.
gi 697052506 146 LRA-LQEAGLK 155
Cdd:cd13574  130 PRAmLRQAGIT 140
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
61-180 3.75e-04

Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate receptor domain GluR0. These domains are found in the GluR0 proteins that have been shown to function as prokaryotic L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. The GluR0 proteins 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: 270218 [Multi-domain]  Cd Length: 218  Bit Score: 41.17  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  61 WVEFPAGPQMLEALNVGSIDLGsTGDIPPIFAQAAGADLVYvgveppkPKAEV---ILVPENSDIKSVADLKGHKVAFQK 137
Cdd:cd00997   44 YVRVDSVSALLAAVAEGEADIA-IAAISITAEREAEFDFSQ-------PIFESglqILVPNTPLINSVNDLYGKRVATVA 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 697052506 138 GSSShnlllralqEAGLKFTDIQPV-YLTPADARAAFQQKNVDA 180
Cdd:cd00997  116 GSTA---------ADYLRRHDIDVVeVPNLEAAYTALQDKDADA 150
PBP2_ThiY cd13651
Substrate binding domain of ABC-type transporters for thiamin biosynthetic pathway ...
64-180 4.02e-04

Substrate binding domain of ABC-type transporters for thiamin biosynthetic pathway intermediates; a member of the type 2 periplasmic binding fold superfamily; ThiY is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport , as well as THI5 which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes. After binding the ligand, they 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. The ThiY/THI5 proteins 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: 270369 [Multi-domain]  Cd Length: 214  Bit Score: 40.80  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  64 FPAGP----QMLEAlnvGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVIlVPENSDIKSVADLKGHKVAFQKGS 139
Cdd:cd13651   37 APADPsdplKLVAA---GKADLAVSYQPQVILARSEGLPVVSVGALVRSPLNSLM-VLKDSGIKSPADLKGKKVGYSVLG 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 697052506 140 SSHNLLLRALQEAGLKFTDIQPVYLTpADARAAFQQKNVDA 180
Cdd:cd13651  113 FEEALLDTMLKAAGGDPSDVELVNVG-FDLSPALTSGQVDA 152
PBP2_GluB cd13690
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ...
114-180 7.18e-04

Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein fold; This group includes periplasmic glutamate-binding domain GluB from Corynebacterium efficiens and its related proteins. The GluB 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: 270408 [Multi-domain]  Cd Length: 231  Bit Score: 40.33  E-value: 7.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052506 114 ILVPENSD-IKSVADLKGHKVAFQKGSSShnllLRALQEAGLKFTDIQPVylTPADARAAFQQKNVDA 180
Cdd:cd13690  102 LLVRAGSKiITSPEDLNGKTVCTAAGSTS----ADNLKKNAPGATIVTRD--NYSDCLVALQQGRVDA 163
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
113-211 1.01e-03

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: 39.61  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 113 VILVP-ENSDIKSVADLKGHKVAFQKGsSSHNLLLRALQeaglKFTDIQPvYLTPADARAAFQQKNVDAwAIWDPYYSAA 191
Cdd:cd13626   89 QIIVKkDNTIIKSLEDLKGKVVGVSLG-SNYEEVARDLA----NGAEVKA-YGGANDALQDLANGRADA-TLNDRLAALY 161
                         90       100
                 ....*....|....*....|
gi 697052506 192 LLQggvrvlKDGTTLKQTGS 211
Cdd:cd13626  162 ALK------NSNLPLKIVGD 175
PBP2_lipoprotein_MetQ_like cd13526
The periplasmic-binding component of ABC-type methionine uptake transporter system and its ...
30-168 1.15e-03

The periplasmic-binding component of ABC-type methionine uptake transporter system and its related lipoproteins; the type 2 periplasmic-binding protein fold; This family represents the periplasmic substrate-binding domain of ATP-binding cassette (ABC) transporter involved in uptake of methionine (MetQ) and its related homologs. Members of the MetQ-like family include the 32-kilodalton lipoprotein (Tp32) from Treponema pallidum, the membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus, and Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus. They all function as a receptor for methionine. 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. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270244  Cd Length: 228  Bit Score: 39.60  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSVSMVLAKSHQLLEKRFPDTKFswVEFPAGPQMLEALNVGSIDLGSTGDIPPI--FAQAAGADLVYVGvepP 107
Cdd:cd13526    2 LKIGVTAGPSADVVEAAKKEAKKKGYELEL--VVFTDYVAPNEALNDGSIDANFFQHVPFLdqFNKERNGDLVKVG---K 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 697052506 108 KPKAEVILVPEnsDIKSVADLK-GHKVAFQKGSSSHNLLLRALQEAGL-KFTDIQPVYLTPAD 168
Cdd:cd13526   77 TVIAPIGLYSK--KYKSLDELPdGARIAIPNDPSNGARALLLLEDAGLiKLKDGVGLFATVLD 137
PBP2_TAXI_TRAP_like_3 cd13568
Substrate binding domain of putative TAXI proteins of the tripartite ATP-independent ...
114-180 1.31e-03

Substrate binding domain of putative TAXI proteins of the tripartite ATP-independent periplasmic transporters; the type 2 periplasmic binding protein fold; This subgroup includes uncharacterized periplasmic binding proteins that are related to Thermus thermophilus GluBP (TtGluBP) of TAXI-TRAP family. TRAP transporters are comprised of an SBP (substrate-binding protein) and two unequally sized integral membrane components. Although TtGluBP is predicted to be an L-glutamate and/or an L-glutamine-binding protein, the substrate spectrum of TAXI proteins remains to be defined. A sequence-homology search also shows that TtGluBP shares low sequence homology with putative immunogenic proteins of uncharacterized function.


Pssm-ID: 270286 [Multi-domain]  Cd Length: 289  Bit Score: 39.98  E-value: 1.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052506 114 ILVPENSDIKSVADLKGHKVAF-QKGSSSHNLLLRALQEAGLKFTDIQPVYLTPADARA-AFQQKNVDA 180
Cdd:cd13568   97 VVARADSGIKSFDDLKGKRVNIgNPGSGQRATMLALLGAKGWTKKDFALAIELKASEQAeALCDGKIDA 165
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
114-194 2.94e-03

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: 38.38  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 114 ILVPENSD--IKSVADLKGHKVAFQKGSSSHNLLLRALQE---AGLKFTDIQPvYLTPADARAAFQQKNVDAWaiWDPYY 188
Cdd:cd01004   91 VLVAKGNPkkIKSPEDLCGKTVAVQTGTTQEQLLQAANKKckaAGKPAIEIQT-FPDQADALQALRSGRADAY--LSDSP 167

                 ....*.
gi 697052506 189 SAALLQ 194
Cdd:cd01004  168 TAAYAV 173
PBP2_polar_AA cd13693
Substrate binding domain of polar amino-acid uptake ABC transporter; the type 2 periplasmic ...
104-196 3.00e-03

Substrate binding domain of polar amino-acid uptake ABC transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of putative polar amino acid ABC transporter. The polar amino-acid 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: 270411 [Multi-domain]  Cd Length: 228  Bit Score: 38.45  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506 104 VEPPKPKAEV-ILVPENSDIKSVADLKGHKVAFQKGSSSHnlllRALQEaglKFtDIQPV-YLTPADARAAFQQKNVDAW 181
Cdd:cd13693   88 VEPYYYRSGGaLLAAKDSGINDWEDLKGKPVCGSQGSYYN----KPLIE---KY-GAQLVaFKGTPEALLALRDGRCVAF 159
                         90
                 ....*....|....*
gi 697052506 182 AIWDPYYSAALLQGG 196
Cdd:cd13693  160 VYDDSTLQLLLQEDG 174
PBP2_Peb1a_like cd13691
Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 ...
113-183 4.85e-03

Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 periplasmic-binding protein fold; This group includes periplasmic aspartate/glutamate binding domain Peb1a and its closely related protein. The Peb1a is an important virulence factor in the food-borne human pathogen Campylobacter jejuni, which has a major role in adherence and host colonization. The Peb1a 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: 270409 [Multi-domain]  Cd Length: 228  Bit Score: 37.82  E-value: 4.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 697052506 113 VILVPENSDIKSVADLKGHKVAFQKGSSSHNLLLRALQEAGLKFTDIQpvYLTPADARAAFQQKNVDAWAI 183
Cdd:cd13691   99 GVLVEKSSGIKSLADLKGKTVGVASGATTKKALEAAAKKIGIGVSFVE--YADYPEIKTALDSGRVDAFSV 167
PBP2_lipoprotein_IlpA_like cd13598
Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar ...
30-171 7.07e-03

Toll-like receptor 2-activating lipoprotein IlpA from Vibrio vulnificus and similar lipoproteins; the type 2 periplasmic binding protein fold; This group includes the IlpA protein which has both structural and sequential homology to the MetQ family of substrate-binding protein, and thus 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. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270316  Cd Length: 227  Bit Score: 37.33  E-value: 7.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSVSMVLAKSHQLLEKRFPDTKFswVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQ--AAGADLVYVGVEPP 107
Cdd:cd13598    2 IKVGVIRGPDAQIWEVVQKVAKEKGLDVEL--VTFNDYAQPNEALAAGDLDANAFQHKPYLDAQikARGYKLVIVGNTFV 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697052506 108 KPKAEVilvpeNSDIKSVADLK-GHKVAFQKGSSSHNLLLRALQEAGL-KFTDIQPVYLTPADARA 171
Cdd:cd13598   80 YPIGLY-----SKKIKSLAELPnGATVAIPNDPSNEGRALLLLQKEGLiKLKDGVGLLATVRDIAE 140
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
30-123 9.88e-03

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: 36.84  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052506  30 LRIGYQKGSVSMvlakshQLLEKRFPDTKFswVEFPAGPQMLEALNVGSIDLGSTgDIPPIFAQAAGADLVYVGVEPPKP 109
Cdd:cd13530  108 KKVGVQAGTTGE------DYAKKNLPNAEV--VTYDNYPEALQALKAGRIDAVIT-DAPVAKYYVKKNGPDLKVVGEPLT 178
                         90
                 ....*....|....*.
gi 697052506 110 KAE--VILVPENSDIK 123
Cdd:cd13530  179 PEPygIAVRKGNPELL 194
 
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.
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