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Conserved domains on  [gi|1045425042|ref|WP_065497151|]
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MULTISPECIES: ABC transporter substrate-binding protein [Burkholderia]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11431285)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one of a variety of substrates, including ions such as bicarbonate and nitrate; belongs to the type 2 periplasmic binding protein (PBP2) family

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
36-334 6.48e-22

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


:

Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 93.92  E-value: 6.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  36 PQAAQAEGRIRIAEQFGVVYLMLNVARDQQLIEKEGrkagldIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVwd 115
Cdd:COG0715    15 AAAAAEKVTLRLGWLPNTDHAPLYVAKEKGYFKKEG------LDVELVEFAGGAAALEALAAGQADFGVAGAPPALAA-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 116 RTRGrQNVKGVASLGNFP--YYLVSTNPNVRTIADLSAKdRIAVPavGVSVQSRVLQYAAAKQwgdrQFDRLDALTQAIP 193
Cdd:COG0715    87 RAKG-APVKAVAALSQSGgnALVVRKDSGIKSLADLKGK-KVAVP--GGSTSHYLLRALLAKA----GLDPKDVEIVNLP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 194 HPDATAAIVANSnvITGHFGNPPFqEQELAGNPNAHVVLNSYDVLGGPSsATVLYATEAFRRDNPKTYRAFVAALADAAQ 273
Cdd:COG0715   159 PPDAVAALLAGQ--VDAAVVWEPF-ESQAEKKGGGRVLADSADLVPGYP-GDVLVASEDFLEENPEAVKAFLRALLKAWA 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045425042 274 QIAADPERAADVYIRANGskIDRALLLKILRNP----QVQFKIAPQNTLRLAQFMYRTGAIRHEP 334
Cdd:COG0715   235 WAAANPDEAAAILAKATG--LDPEVLAAALEGDlrldPPLGAPDPARLQRVADFLVELGLLPKDV 297
 
Name Accession Description Interval E-value
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
36-334 6.48e-22

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 93.92  E-value: 6.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  36 PQAAQAEGRIRIAEQFGVVYLMLNVARDQQLIEKEGrkagldIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVwd 115
Cdd:COG0715    15 AAAAAEKVTLRLGWLPNTDHAPLYVAKEKGYFKKEG------LDVELVEFAGGAAALEALAAGQADFGVAGAPPALAA-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 116 RTRGrQNVKGVASLGNFP--YYLVSTNPNVRTIADLSAKdRIAVPavGVSVQSRVLQYAAAKQwgdrQFDRLDALTQAIP 193
Cdd:COG0715    87 RAKG-APVKAVAALSQSGgnALVVRKDSGIKSLADLKGK-KVAVP--GGSTSHYLLRALLAKA----GLDPKDVEIVNLP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 194 HPDATAAIVANSnvITGHFGNPPFqEQELAGNPNAHVVLNSYDVLGGPSsATVLYATEAFRRDNPKTYRAFVAALADAAQ 273
Cdd:COG0715   159 PPDAVAALLAGQ--VDAAVVWEPF-ESQAEKKGGGRVLADSADLVPGYP-GDVLVASEDFLEENPEAVKAFLRALLKAWA 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045425042 274 QIAADPERAADVYIRANGskIDRALLLKILRNP----QVQFKIAPQNTLRLAQFMYRTGAIRHEP 334
Cdd:COG0715   235 WAAANPDEAAAILAKATG--LDPEVLAAALEGDlrldPPLGAPDPARLQRVADFLVELGLLPKDV 297
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
45-260 7.62e-14

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: 69.62  E-value: 7.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  45 IRIAEQFGVVYLMLNVARDQQLIEKEGRKagldIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVwdrTRGRQNVK 124
Cdd:cd01008     2 VRIGYQAGPLAGPLIVAKEKGLFEKEKEG----IDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLA---AAGGVPVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 125 GVASLGNFPYY---LVSTNPNVRTIADLSAKdRIAVPAVGVSVQSrVLQYAAAKQWGDRQFDRLDaltqaIPHPDATAAI 201
Cdd:cd01008    75 LIAALSRSPNGngiVVRKDSGITSLADLKGK-KIAVTKGTTGHFL-LLKALAKAGLSVDDVELVN-----LGPADAAAAL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1045425042 202 VanSNVITGHFGNPPFQEQELAGNpNAHVVLNSYDVLGgpSSATVLYATEAFRRDNPKT 260
Cdd:cd01008   148 A--SGDVDAWVTWEPFLSLAEKGG-DARIIVDGGGLPY--TDPSVLVARRDFVEENPEA 201
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
60-341 1.39e-11

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: 64.30  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  60 VARDQQLIEKEGRKagldIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVWDRTRGRQNVKGVASLGNFPyYLVST 139
Cdd:TIGR01728  15 LAKEKGLLEKELGK----TKVEWVEFPAGPPALEALGAGSLDFGYIGPGPALFAYAAGADIKAVGLVSDNKATA-IVVIK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 140 NPNVRTIADLSAKdRIAVP--AVGVSVQSRVLQYAAAKQwGDRQFDRLDaltqaipHPDATAAIVANSNVITGHFGNPPF 217
Cdd:TIGR01728  90 GSPIRTVADLKGK-RIAVPkgGSGHDLLLRALLKAGLSG-DDVTILYLG-------PSDARAAFAAGQVDAWAIWEPWGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 218 QEQELAGnpnAHVVLNsYDVLGGPSSATVLYATEAFRRDNPKTYRAFVAALADAAQQIAADPERAADVYIRAngSKIDRA 297
Cdd:TIGR01728 161 ALVEEGG---ARVLAN-GEGIGLPGQPGFLVVRREFAEAHPEQVQRVLKVLVKARKWAEENPEESAKILAKE--LGLSQA 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1045425042 298 LLL------KILRNPQV--QFKIAPQNTlrlAQFMYRTGAIRhEPTSWRDYF 341
Cdd:TIGR01728 235 VVEetvlnrRFLRVEVIsdAVVDALQAM---ADFFYAAGLLK-KKPDLKDAV 282
tauA PRK11480
taurine transporter substrate binding subunit; Provisional
79-178 1.85e-03

taurine transporter substrate binding subunit; Provisional


Pssm-ID: 183158  Cd Length: 320  Bit Score: 39.59  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  79 KVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVWDRTRGRQNVKGVASLGNFPYYLVSTnpNVRTIADLSAKdRIAVP 158
Cdd:PRK11480   52 TVDWRKFDSGASIVRALASGDVQIGNLGSSPLAVAASQQVPIEVFLLASKLGNSEALVVKK--TISKPEDLIGK-RIAVP 128
                          90       100
                  ....*....|....*....|
gi 1045425042 159 AVGVSVQSRVlqyAAAKQWG 178
Cdd:PRK11480  129 FISTTHYSLL---AALKHWG 145
 
Name Accession Description Interval E-value
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
36-334 6.48e-22

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 93.92  E-value: 6.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  36 PQAAQAEGRIRIAEQFGVVYLMLNVARDQQLIEKEGrkagldIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVwd 115
Cdd:COG0715    15 AAAAAEKVTLRLGWLPNTDHAPLYVAKEKGYFKKEG------LDVELVEFAGGAAALEALAAGQADFGVAGAPPALAA-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 116 RTRGrQNVKGVASLGNFP--YYLVSTNPNVRTIADLSAKdRIAVPavGVSVQSRVLQYAAAKQwgdrQFDRLDALTQAIP 193
Cdd:COG0715    87 RAKG-APVKAVAALSQSGgnALVVRKDSGIKSLADLKGK-KVAVP--GGSTSHYLLRALLAKA----GLDPKDVEIVNLP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 194 HPDATAAIVANSnvITGHFGNPPFqEQELAGNPNAHVVLNSYDVLGGPSsATVLYATEAFRRDNPKTYRAFVAALADAAQ 273
Cdd:COG0715   159 PPDAVAALLAGQ--VDAAVVWEPF-ESQAEKKGGGRVLADSADLVPGYP-GDVLVASEDFLEENPEAVKAFLRALLKAWA 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1045425042 274 QIAADPERAADVYIRANGskIDRALLLKILRNP----QVQFKIAPQNTLRLAQFMYRTGAIRHEP 334
Cdd:COG0715   235 WAAANPDEAAAILAKATG--LDPEVLAAALEGDlrldPPLGAPDPARLQRVADFLVELGLLPKDV 297
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
45-260 7.62e-14

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: 69.62  E-value: 7.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  45 IRIAEQFGVVYLMLNVARDQQLIEKEGRKagldIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVwdrTRGRQNVK 124
Cdd:cd01008     2 VRIGYQAGPLAGPLIVAKEKGLFEKEKEG----IDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLA---AAGGVPVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 125 GVASLGNFPYY---LVSTNPNVRTIADLSAKdRIAVPAVGVSVQSrVLQYAAAKQWGDRQFDRLDaltqaIPHPDATAAI 201
Cdd:cd01008    75 LIAALSRSPNGngiVVRKDSGITSLADLKGK-KIAVTKGTTGHFL-LLKALAKAGLSVDDVELVN-----LGPADAAAAL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1045425042 202 VanSNVITGHFGNPPFQEQELAGNpNAHVVLNSYDVLGgpSSATVLYATEAFRRDNPKT 260
Cdd:cd01008   148 A--SGDVDAWVTWEPFLSLAEKGG-DARIIVDGGGLPY--TDPSVLVARRDFVEENPEA 201
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
60-341 1.39e-11

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: 64.30  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  60 VARDQQLIEKEGRKagldIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVWDRTRGRQNVKGVASLGNFPyYLVST 139
Cdd:TIGR01728  15 LAKEKGLLEKELGK----TKVEWVEFPAGPPALEALGAGSLDFGYIGPGPALFAYAAGADIKAVGLVSDNKATA-IVVIK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 140 NPNVRTIADLSAKdRIAVP--AVGVSVQSRVLQYAAAKQwGDRQFDRLDaltqaipHPDATAAIVANSNVITGHFGNPPF 217
Cdd:TIGR01728  90 GSPIRTVADLKGK-RIAVPkgGSGHDLLLRALLKAGLSG-DDVTILYLG-------PSDARAAFAAGQVDAWAIWEPWGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 218 QEQELAGnpnAHVVLNsYDVLGGPSSATVLYATEAFRRDNPKTYRAFVAALADAAQQIAADPERAADVYIRAngSKIDRA 297
Cdd:TIGR01728 161 ALVEEGG---ARVLAN-GEGIGLPGQPGFLVVRREFAEAHPEQVQRVLKVLVKARKWAEENPEESAKILAKE--LGLSQA 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1045425042 298 LLL------KILRNPQV--QFKIAPQNTlrlAQFMYRTGAIRhEPTSWRDYF 341
Cdd:TIGR01728 235 VVEetvlnrRFLRVEVIsdAVVDALQAM---ADFFYAAGLLK-KKPDLKDAV 282
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
60-262 5.49e-11

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: 61.44  E-value: 5.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  60 VARDQQLIEKEGrkagldIKVDWVRLSGGAAVNDALLSGAVDIAGAGV-GPLLTvwdrTRGRQ-NVKGVASL---GNfpY 134
Cdd:cd13553    17 VAKEKGFFEKEG------LDVELVKFPSWADLRDALAAGELDAAHVLApMPAAA----TYGKGaPIKVVAGLhrnGS--A 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 135 YLVSTNPNVRTIADLSAKdRIAVPAVGvSVQSRVLQYAAAKQ---WGDrqfdrlDALTQAIPHPDATAAIVANSnvITGH 211
Cdd:cd13553    85 IVVSKDSGIKSVADLKGK-TIAVPFPG-STHDVLLRYWLAAAgldPGK------DVEIVVLPPPDMVAALAAGQ--IDAY 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1045425042 212 FGNPPFQEQ-ELAGnpNAHVVLNSYDVLGGpSSATVLYATEAFRRDNPKTYR 262
Cdd:cd13553   155 CVGEPWNARaVAEG--VGRVLADSGDIWPG-HPCCVLVVREDFLEENPEAVQ 203
PBP2_taurine cd13560
Taurine-binding periplasmic protein; the type 2 periplasmic binding protein fold; This ...
60-178 2.80e-08

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: 53.46  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  60 VARDQQLIEKEgrkagLDIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVwdrTRGRQNVKGV---ASLGNFPYYL 136
Cdd:cd13560    15 VAKADGLLEKA-----LGVKVNWRKFDSGADVNAAMASGSIDIGLLGSPPAAVA---IAAGLPIEVIwiaDVIGDAEALV 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1045425042 137 VSTNPNVRTIADLSAKdRIAVPAVGVSvqsrvlQY---AAAKQWG 178
Cdd:cd13560    87 VRKGSGIKSLKDLAGK-KVAVPFGSTA------HYsllAALKHAG 124
PBP2_sulfate_ester_like cd13555
Sulfate ester binding protein-like, the type 2 periplasmic binding protein fold; This ...
60-258 3.41e-08

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: 53.88  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  60 VARDQQLIEKEGRKAGldIKVDWVRLSG-GAAVNDALLSGAVDIAGAGVGPLLTvwdrtrGRQN---VKGVAS--LGNFP 133
Cdd:cd13555    23 VAHEKGWLEEEFAKDG--IKVEWVFFKGaGPAVNEAFANGQIDFAVYGDLPAII------GRAAgldTKLLLSsgSGNNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 134 YYLVSTNPNVRTIADLSAKdRIAVPAvGVSVQSRVLQYAAAKQWGDRQFDRLDAltqaipHPDATAAIVANSNViTGHFG 213
Cdd:cd13555    95 YLVVPPDSTIKSVKDLKGK-KVAVQK-GTAWQLTFLRILAKNGLSEKDFKIVNL------DAQDAQAALASGDV-DAAFT 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1045425042 214 NPPFQEQELAGNpnAHVVLNSYDVLGGPSSATVLYATEAFRRDNP 258
Cdd:cd13555   166 GYEALKLEDQGA--GKIIWSTKDKPEDWTTQSGVWARTDFIKENP 208
TauA COG4521
ABC-type taurine transport system, periplasmic component [Inorganic ion transport and ...
37-178 4.42e-08

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


Pssm-ID: 443595 [Multi-domain]  Cd Length: 332  Bit Score: 54.11  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  37 QAAQAEGRIRIAEQFGVVYLMlnVARDQQLIEKEgrkagLDIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVWdr 116
Cdd:COG4521    22 AAAAAAKEVTIGYQTIPNPEL--VAKADGALEKA-----LGAKVNWRKFDSGADVITALASGDVDIGSIGSSPFAAAL-- 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045425042 117 TRGrQNVKGVA---SLGNFPYYLVSTNPNVRTIADLSAKdRIAVPAVGVSvqsrvlQY---AAAKQWG 178
Cdd:COG4521    93 SRG-LPIEVIWiadVIGDAEALVVRNGSGITSPKDLKGK-KIAVPFGSTS------HYsllAALKHAG 152
PBP2_SsuA_like_5 cd13562
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
45-157 1.44e-06

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: 48.65  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  45 IRIAEQFGVVYLMLNVARDQQLIEKEGRKAGLDIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTvwdrtrGRQN-- 122
Cdd:cd13562     2 IRIGFQPIPPYAPILVAKQKGWLEEELKKAGADVGVKWSQFSAGPPVNEAFAAGELDVGLLGDTPAII------GRAAgq 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1045425042 123 ---VKGVASLGNFPY-YLVSTNPNVRTIADLSAKdRIAV 157
Cdd:cd13562    76 dtrIVGLASTGPKALaLVVRKDSAIKSVKDLKGK-KVAT 113
PBP2_SsuA_like_2 cd13558
Putative substrate binding domain of sulfonate binding protein, the type 2 periplasmic binding ...
64-176 1.48e-06

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: 48.82  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  64 QQLIEKEGRKAGLDIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVwdrTRGRQNVKGVASLGNFPY---YLVSTN 140
Cdd:cd13558    12 RALLEAAGELDGLPYKIEWAEFQGGAPLLEALRAGALDIGGAGDTPPLFA---AAAGAPIKIVAALRGDVNgqaLLVPKD 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1045425042 141 PNVRTIADLSAKdRIAVpavgvsVQSRVLQYAAAKQ 176
Cdd:cd13558    89 SPIRSVADLKGK-RVAY------VRGSISHYLLLKA 117
PBP2_SsuA cd13557
Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic ...
58-258 5.48e-05

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: 44.21  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  58 LNVARDQQLIEKegRKAGLDIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPllTVWDRTRGrQNVKGVASLGNFPY--- 134
Cdd:cd13557    12 LVLLKARGELEK--RLKPLGVKVTWSEFPAGPQLLEALNVGSIDFGSTGDTP--PIFAQAAG-APLVYVAVEPPTPKgea 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042 135 YLVSTNPNVRTIADLSAKdRIAVpAVGVSVQS---RVLQyAAAKQWGDRQFDRLdaltqaiPHPDATAAIvANSNVITGH 211
Cdd:cd13557    87 ILVPKDSPIKTVADLKGK-KIAF-QKGSSAHYllvKALE-KAGLTLDDIEPVYL-------SPADARAAF-EQGQVDAWA 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1045425042 212 FGNPPFQEQELAGNPnahVVLNSYDVLGGpsSATVLYATEAFRRDNP 258
Cdd:cd13557   156 IWDPYLAAAELTGGA---RVLADGEGLVN--NRSFYLAARDFAKDNP 197
PBP2_SsuA_like_1 cd13556
Substrate binding domain of putative sulfonate binding protein, a member of the type 2 ...
60-157 1.30e-04

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: 42.84  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  60 VARDQQLIEKEGRKAGldIKVDWVRLSGGAAVNDALLSGAVDIAG-AGVGPLLTvwdRTRGRQnVKG--VASLGNFPYYL 136
Cdd:cd13556    15 VLKKFGWLEKEFQKDG--VKVTWVLSQGSNKALEFLNSGSVDFGStAGLAALLA---KANGNP-IKTvyVYSRPEWTALV 88
                          90       100
                  ....*....|....*....|.
gi 1045425042 137 VSTNPNVRTIADLSAKdRIAV 157
Cdd:cd13556    89 VRKDSPIRSVADLKGK-KVAV 108
tauA PRK11480
taurine transporter substrate binding subunit; Provisional
79-178 1.85e-03

taurine transporter substrate binding subunit; Provisional


Pssm-ID: 183158  Cd Length: 320  Bit Score: 39.59  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  79 KVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVWDRTRGRQNVKGVASLGNFPYYLVSTnpNVRTIADLSAKdRIAVP 158
Cdd:PRK11480   52 TVDWRKFDSGASIVRALASGDVQIGNLGSSPLAVAASQQVPIEVFLLASKLGNSEALVVKK--TISKPEDLIGK-RIAVP 128
                          90       100
                  ....*....|....*....|
gi 1045425042 159 AVGVSVQSRVlqyAAAKQWG 178
Cdd:PRK11480  129 FISTTHYSLL---AALKHWG 145
PBP2_SsuA_like_3 cd13559
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
62-158 4.21e-03

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: 38.17  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045425042  62 RDQQLIEK----EGRKAGLDIKVDWVRLSGGAAVNDALLSGAVDIAGAGVGPLLTVWDRTRGRQNVKGV-------ASLG 130
Cdd:cd13559    21 RELGLLEKylpeLGKYKDVEYEIEWQDFTSGAPLTNEMVAGKLDIGAMGDFPGLLNGVKFQTSAGYRSVfiaflggSPDG 100
                          90       100
                  ....*....|....*....|....*...
gi 1045425042 131 NFPYYLVSTNPNVRTIADLSAKDrIAVP 158
Cdd:cd13559   101 SGNAIVVPKDSPVNSLDDLKGKT-VSVP 127
MopB_Formate-Dh-H cd02753
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
89-136 8.15e-03

Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239154 [Multi-domain]  Cd Length: 512  Bit Score: 37.96  E-value: 8.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1045425042  89 AAVNDALLSGAVDIAGAGVGPLltvwdrtRGRQNVKGVASLGNFPYYL 136
Cdd:cd02753   301 ALSNLALLTGNIGRPGTGVNPL-------RGQNNVQGACDMGALPNVL 341
 
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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