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Conserved domains on  [gi|1348967809|ref|WP_104470172|]
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ABC transporter substrate-binding protein [Acinetobacter indicus]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194283)

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
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
8-239 8.83e-67

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: 208.97  E-value: 8.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   8 ELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAHCLSAMLPAAALGTdqlGIPLQTPLV 87
Cdd:cd13553     1 TLRIGYLPITDHAPLLVAKEKGFFEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYGK---GAPIKVVAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  88 LSTNQAYISLSqslcfelgiqpEDDAAHIAKKLinahqqRPIQLAHVFHASIHHYCLREWLALADPILAKNIQLITLPPP 167
Cdd:cd13553    78 LHRNGSAIVVS-----------KDSGIKSVADL------KGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKDVEIVVLPPP 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348967809 168 YMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRA 239
Cdd:cd13553   141 DMVAALAAGQIDAYCVGEPWNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKALVEA 212
 
Name Accession Description Interval E-value
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
8-239 8.83e-67

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: 208.97  E-value: 8.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   8 ELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAHCLSAMLPAAALGTdqlGIPLQTPLV 87
Cdd:cd13553     1 TLRIGYLPITDHAPLLVAKEKGFFEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYGK---GAPIKVVAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  88 LSTNQAYISLSqslcfelgiqpEDDAAHIAKKLinahqqRPIQLAHVFHASIHHYCLREWLALADPILAKNIQLITLPPP 167
Cdd:cd13553    78 LHRNGSAIVVS-----------KDSGIKSVADL------KGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKDVEIVVLPPP 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348967809 168 YMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRA 239
Cdd:cd13553   141 DMVAALAAGQIDAYCVGEPWNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKALVEA 212
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
5-240 7.60e-60

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


Pssm-ID: 463863  Cd Length: 254  Bit Score: 192.56  E-value: 7.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   5 EKTELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAHCLSAMLPAAALGTDQLGIPLQT 84
Cdd:pfam13379   4 EKTSLKLGFIPLTDAAPLIVAAEKGFFAKYGLTVELSKQASWAETRDALVAGELDAAHVLTPMPYLITLGIGGAKVPMIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  85 PLVLSTNQAYISLSQSLCFELGIQPEDDAAHIAKKlinAHQQRPIQLAHVFHASIHHYCLREWLALA--DPilAKNIQLI 162
Cdd:pfam13379  84 LASLNLNGQAITLANKYADKGVRDAAALKDLVGAY---KASGKPFKFAVTFPGSTHDLWLRYWLAAGglDP--DADVKLV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348967809 163 TLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRAQ 240
Cdd:pfam13379 159 VVPPPQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKDHPEKVLGVRADWVDKNPNAARALVKALIEAT 236
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
4-259 4.35e-39

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 140.14  E-value: 4.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   4 LEKTELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAHCLSAMLPAAALGtdqlGIPLQ 83
Cdd:COG0715    19 AEKVTLRLGWLPNTDHAPLYVAKEKGYFKKEGLDVELVEFAGGAAALEALAAGQADFGVAGAPPALAARAK----GAPVK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  84 TPLVL--STNQAYISLSQSlcfelGIQ-PEDdaahIAKKLINahqqrpiqlahVFHASIHHYCLREWLALADpILAKNIQ 160
Cdd:COG0715    95 AVAALsqSGGNALVVRKDS-----GIKsLAD----LKGKKVA-----------VPGGSTSHYLLRALLAKAG-LDPKDVE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 161 LITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRAQ 240
Cdd:COG0715   154 IVNLPPPDAVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVPGYPGDVLVASEDFLEENPEAVKAFLRALLKAW 233
                         250
                  ....*....|....*....
gi 1348967809 241 AELQqlEDVQAVWQMLNEA 259
Cdd:COG0715   234 AWAA--ANPDEAAAILAKA 250
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
9-241 7.71e-04

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: 40.81  E-value: 7.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   9 LQIGYIPLLDCVAILwAKQRGFFADAG--LNVELLKEPSWASLRDRLAFGFMDAAH--CLSAMLPAAAlgtdqlGIPLQt 84
Cdd:TIGR01728   1 VRIGYQKNGHSALAL-AKEKGLLEKELgkTKVEWVEFPAGPPALEALGAGSLDFGYigPGPALFAYAA------GADIK- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  85 plvlstnqayislsqslcfELGIQPEDDAAHIAKKlinahQQRPIQ---------LAHVFHASIHHYCLRewlALADPIL 155
Cdd:TIGR01728  73 -------------------AVGLVSDNKATAIVVI-----KGSPIRtvadlkgkrIAVPKGGSGHDLLLR---ALLKAGL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 156 AKN-IQLITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTS 234
Cdd:TIGR01728 126 SGDdVTILYLGPSDARAAFAAGQVDAWAIWEPWGSALVEEGGARVLANGEGIGLPGQPGFLVVRREFAEAHPEQVQRVLK 205

                  ....*..
gi 1348967809 235 AIQRAQA 241
Cdd:TIGR01728 206 VLVKARK 212
 
Name Accession Description Interval E-value
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
8-239 8.83e-67

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: 208.97  E-value: 8.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   8 ELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAHCLSAMLPAAALGTdqlGIPLQTPLV 87
Cdd:cd13553     1 TLRIGYLPITDHAPLLVAKEKGFFEKEGLDVELVKFPSWADLRDALAAGELDAAHVLAPMPAAATYGK---GAPIKVVAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  88 LSTNQAYISLSqslcfelgiqpEDDAAHIAKKLinahqqRPIQLAHVFHASIHHYCLREWLALADPILAKNIQLITLPPP 167
Cdd:cd13553    78 LHRNGSAIVVS-----------KDSGIKSVADL------KGKTIAVPFPGSTHDVLLRYWLAAAGLDPGKDVEIVVLPPP 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348967809 168 YMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRA 239
Cdd:cd13553   141 DMVAALAAGQIDAYCVGEPWNARAVAEGVGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKALVEA 212
NMT1_2 pfam13379
NMT1-like family; This family is closely related to the pfam09084 family.
5-240 7.60e-60

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


Pssm-ID: 463863  Cd Length: 254  Bit Score: 192.56  E-value: 7.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   5 EKTELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAHCLSAMLPAAALGTDQLGIPLQT 84
Cdd:pfam13379   4 EKTSLKLGFIPLTDAAPLIVAAEKGFFAKYGLTVELSKQASWAETRDALVAGELDAAHVLTPMPYLITLGIGGAKVPMIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  85 PLVLSTNQAYISLSQSLCFELGIQPEDDAAHIAKKlinAHQQRPIQLAHVFHASIHHYCLREWLALA--DPilAKNIQLI 162
Cdd:pfam13379  84 LASLNLNGQAITLANKYADKGVRDAAALKDLVGAY---KASGKPFKFAVTFPGSTHDLWLRYWLAAGglDP--DADVKLV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348967809 163 TLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRAQ 240
Cdd:pfam13379 159 VVPPPQMVANLRAGNIDGFCVGEPWNARAVAEGIGVTAATTGELWKDHPEKVLGVRADWVDKNPNAARALVKALIEAT 236
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
4-259 4.35e-39

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


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 140.14  E-value: 4.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   4 LEKTELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAHCLSAMLPAAALGtdqlGIPLQ 83
Cdd:COG0715    19 AEKVTLRLGWLPNTDHAPLYVAKEKGYFKKEGLDVELVEFAGGAAALEALAAGQADFGVAGAPPALAARAK----GAPVK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  84 TPLVL--STNQAYISLSQSlcfelGIQ-PEDdaahIAKKLINahqqrpiqlahVFHASIHHYCLREWLALADpILAKNIQ 160
Cdd:COG0715    95 AVAALsqSGGNALVVRKDS-----GIKsLAD----LKGKKVA-----------VPGGSTSHYLLRALLAKAG-LDPKDVE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 161 LITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRAQ 240
Cdd:COG0715   154 IVNLPPPDAVAALLAGQVDAAVVWEPFESQAEKKGGGRVLADSADLVPGYPGDVLVASEDFLEENPEAVKAFLRALLKAW 233
                         250
                  ....*....|....*....
gi 1348967809 241 AELQqlEDVQAVWQMLNEA 259
Cdd:COG0715   234 AWAA--ANPDEAAAILAKA 250
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
8-239 1.75e-19

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: 85.42  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   8 ELQIGYIPLLDCVAILWAKQRGFFADA--GLNVELLKEPSWASLRDRLAFGFMDAAHCLSAMLPAAALGtdqlGIPLQTP 85
Cdd:cd01008     1 TVRIGYQAGPLAGPLIVAKEKGLFEKEkeGIDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLAAAG----GVPVVLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  86 LVLSTNQAYISLsqslcfelGIQPEDDAAHIA----KKLinahqqrpiqlAHVFhASIHHYCLREWLALADpILAKNIQL 161
Cdd:cd01008    77 AALSRSPNGNGI--------VVRKDSGITSLAdlkgKKI-----------AVTK-GTTGHFLLLKALAKAG-LSVDDVEL 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348967809 162 ITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQvIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRA 239
Cdd:cd01008   136 VNLGPADAAAALASGDVDAWVTWEPFLSLAEKGGDARIIVDGGG-LPYTDPSVLVARRDFVEENPEAVKALLKALVEA 212
PBP2_taurine cd13560
Taurine-binding periplasmic protein; the type 2 periplasmic binding protein fold; This ...
137-245 1.16e-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: 54.62  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 137 ASIHHYCLREWLALADpILAKNIQLITLPPPYMVEAISQQQIDGFCVGEPwnTQAELQGYSKILLSGQQV----IPqVAD 212
Cdd:cd13560   109 GSTAHYSLLAALKHAG-VDPGKVKILDMQPPEIVAAWQRGDIDAAYVWEP--ALSQLKKNGKVLLSSKDLakkgIL-TFD 184
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1348967809 213 kVLAVTAEWAAQHPNTLNAMTSAIQRAQAELQQ 245
Cdd:cd13560   185 -VWVVRKDFAEKYPDVVAAFLKALGDAVDLYRN 216
PBP2_ThiY_THI5_like_1 cd13652
Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 ...
7-239 1.58e-08

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: 54.32  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   7 TELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAhclsAMLPAAA-LGTDQLGIPLQ-T 84
Cdd:cd13652     2 GKVKFGQIPISDFAPVYIAAEKGYFKEEGLDVEITRFASGAEILAALASGQVDVA----GSSPGASlLGALARGADLKiV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  85 PLVLSTNQAYISLSQSLCFELGIQ-PED-DAAHIAkklINAHqqrpiqlahvfhASIHHYCLREWLALADPILAKnIQLI 162
Cdd:cd13652    78 AEGLGTTPGYGPFAIVVRADSGITsPADlVGKKIA---VSTL------------TNILEYTTNAYLKKNGLDPDK-VEFV 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348967809 163 TLPPPYMVEAISQQQIDGFCVGEPWNTQAeLQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQRA 239
Cdd:cd13652   142 EVAFPQMVPALENGNVDAAVLAEPFLSRA-RSSGAKVVASDYADPDPHSQATMVFSADFARENPEVVKKFLRAYLEA 217
PBP2_SsuA_like_4 cd13561
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
8-239 2.73e-08

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: 53.53  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   8 ELQIGYIPLLDCVAILW-AKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMD------AAHCLSAMLPAAALGTDQLGI 80
Cdd:cd13561     1 PIRIGYLPALAVAGPIFiAKEKGLFAKHGLDPDFIEFTSGPPLVAALGSGSLDvgytgpVAFNLPASGQAKVVLINNLEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  81 PLQTPLVLStnQAYISLSQSLCFELGIQPEDDAAHIAKKLinahqqrpiqlahvfhasihhyCLREwlalADpILAKNIQ 160
Cdd:cd13561    81 ATASLIVRA--DSGIASIADLKGKKIGTPSGTTADVALDL----------------------ALRK----AG-LSEKDVQ 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 161 LITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGY-SKILLSGQQVIPQVADKV-LAVTAEWAAQHPNTLNAMTSAIQR 238
Cdd:cd13561   132 IVNMDPAEIVTAFTSGSVDAAALWAPNTATIKEKVPgAVELADNSDFGPDAAVPGaWVARNKYAEENPEELKKFLAALAE 211

                  .
gi 1348967809 239 A 239
Cdd:cd13561   212 A 212
PBP2_SsuA_like_5 cd13562
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
8-239 6.53e-07

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: 49.42  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   8 ELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRD------RLAFGFMDAAhcLSAMLPA-----AALGTD 76
Cdd:cd13562     1 TIRIGFQPIPPYAPILVAKQKGWLEEELKKAGADVGVKWSQFSAgppvneAFAAGELDVG--LLGDTPAiigraAGQDTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  77 QLGIPLQTPLVLSTnqayislsqslcfelgIQPEDDAAHIAKKLinahqqRPIQLAHVFHASIHHYCLrewLALADPILA 156
Cdd:cd13562    79 IVGLASTGPKALAL----------------VVRKDSAIKSVKDL------KGKKVATTKGSYVHHLLV---LVLQEAGLT 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 157 -KNIQLITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSG----QQVIPQVAdkvlavTAEWAAQHPNTLNA 231
Cdd:cd13562   134 iDDVEFINMQQADMNTALTNGDIDAAVIWEPLITKLLSDGVVRVLRDGtgikDGLNVIVA------RGPLIEQNPEVVKA 207

                  ....*...
gi 1348967809 232 MTSAIQRA 239
Cdd:cd13562   208 LLKAYQRG 215
PBP2_SsuA_like_6 cd13563
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ...
8-239 8.03e-07

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: 49.16  E-value: 8.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   8 ELQIGYIPLLDCVAILWAKQRGFFADAGLNVELLKEPSWASLRDRLAFGFMDAAhclsamlpaaalgtdqlgiplqtplV 87
Cdd:cd13563     1 PLKIGISTWPGYGPWYLADEKGFFKKEGLDVELVWFESYSDSMAALASGQIDAA-------------------------A 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  88 LSTNQAYISLSQSLCFELGIQPEDDA---AHIAKKLINAHQQ-RPIQLAhVFHASIHHYclreWLALAdpiLAKN----- 158
Cdd:cd13563    56 TTLDDALAMAAKGVPVKIVLVLDNSNgadGIVAKPGIKSIADlKGKTVA-VEEGSVSHF----LLLNA---LEKAgltek 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 159 -IQLITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQvIPQVADKVLAVTAEWAAQHPNTLNAMTSAIQ 237
Cdd:cd13563   128 dVKIVNMTAGDAGAAFIAGQVDAAVTWEPWLSNALKRGKGKVLVSSAD-TPGLIPDVLVVREDFIKKNPEAVKAVVKAWF 206

                  ..
gi 1348967809 238 RA 239
Cdd:cd13563   207 DA 208
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
9-241 7.71e-04

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: 40.81  E-value: 7.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809   9 LQIGYIPLLDCVAILwAKQRGFFADAG--LNVELLKEPSWASLRDRLAFGFMDAAH--CLSAMLPAAAlgtdqlGIPLQt 84
Cdd:TIGR01728   1 VRIGYQKNGHSALAL-AKEKGLLEKELgkTKVEWVEFPAGPPALEALGAGSLDFGYigPGPALFAYAA------GADIK- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809  85 plvlstnqayislsqslcfELGIQPEDDAAHIAKKlinahQQRPIQ---------LAHVFHASIHHYCLRewlALADPIL 155
Cdd:TIGR01728  73 -------------------AVGLVSDNKATAIVVI-----KGSPIRtvadlkgkrIAVPKGGSGHDLLLR---ALLKAGL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 156 AKN-IQLITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVIPQVADKVLAVTAEWAAQHPNTLNAMTS 234
Cdd:TIGR01728 126 SGDdVTILYLGPSDARAAFAAGQVDAWAIWEPWGSALVEEGGARVLANGEGIGLPGQPGFLVVRREFAEAHPEQVQRVLK 205

                  ....*..
gi 1348967809 235 AIQRAQA 241
Cdd:TIGR01728 206 VLVKARK 212
PBP2_SsuA cd13557
Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic ...
137-226 1.09e-03

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: 39.97  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348967809 137 ASIHHYCLREWLALADPILaKNIQLITLPPPYMVEAISQQQIDGFCVGEPWNTQAELQGYSKILLSGQQVI--------- 207
Cdd:cd13557   111 GSSAHYLLVKALEKAGLTL-DDIEPVYLSPADARAAFEQGQVDAWAIWDPYLAAAELTGGARVLADGEGLVnnrsfylaa 189
                          90       100
                  ....*....|....*....|....*....
gi 1348967809 208 -------PQVADKVLA---VTAEWAAQHP 226
Cdd:cd13557   190 rdfakdnPEAIQIVLEelnKAGEWANTNR 218
 
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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