tripartite tricarboxylate transporter substrate binding protein [Sinorhizobium fredii]
Bug family tripartite tricarboxylate transporter substrate binding protein( domain architecture ID 10007023)
Bug (Bordetella uptake gene) family tripartite tricarboxylate transporter (TTT) substrate binding protein is a periplasmic solute-binding (PBP) receptor that is a component of a TTT
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||
TctC | COG3181 | Tripartite-type tricarboxylate transporter, extracytoplasmic receptor component TctC [Energy ... |
1-320 | 3.90e-73 | ||||||
Tripartite-type tricarboxylate transporter, extracytoplasmic receptor component TctC [Energy production and conversion]; : Pssm-ID: 442414 Cd Length: 324 Bit Score: 228.49 E-value: 3.90e-73
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Name | Accession | Description | Interval | E-value | ||||||
TctC | COG3181 | Tripartite-type tricarboxylate transporter, extracytoplasmic receptor component TctC [Energy ... |
1-320 | 3.90e-73 | ||||||
Tripartite-type tricarboxylate transporter, extracytoplasmic receptor component TctC [Energy production and conversion]; Pssm-ID: 442414 Cd Length: 324 Bit Score: 228.49 E-value: 3.90e-73
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PBP2_Bug_TTT | cd07012 | Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains ... |
31-317 | 1.14e-68 | ||||||
Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains the type 2 periplasmic binding fold; The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) proteins present in a number of bacterial species, but mainly in proteobacteria. In eubacteria, at least three families of periplasmic binding-protein dependent transporters are known: the ATP-binding cassette (ABC) transporters, the tripartite ATP-independent periplasmic transporters, and the tripartite tricarboxylate transporters (TTT). Bug proteins are the PBP components of the TTT. Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter. Pssm-ID: 270234 Cd Length: 291 Bit Score: 215.80 E-value: 1.14e-68
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TctC | pfam03401 | Tripartite tricarboxylate transporter family receptor; These probable extra-cytoplasmic solute ... |
47-320 | 3.78e-22 | ||||||
Tripartite tricarboxylate transporter family receptor; These probable extra-cytoplasmic solute receptors are strongly overrepresented in several beta-proteobacteria. This family, formerly known as Bug - Bordetella uptake gene (bug) product - is a family of bacterial tripartite tricarboxylate receptors of the extracytoplasmic solute binding receptor-dependent transporter group of families, distinct from the ABC and TRAP-T families. The TctABC system has been characterized in S. typhimurium, and TctC is the extracytoplasmic tricarboxylate-binding receptor which binds the transporters TctA and TctB, two integral membrane proteins. Complete three-component systems are found only in bacteria. Pssm-ID: 397461 Cd Length: 274 Bit Score: 93.70 E-value: 3.78e-22
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TRAP_TAXI | TIGR02122 | TRAP transporter solute receptor, TAXI family; This family is one of at least three major ... |
1-230 | 9.36e-05 | ||||||
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: 43.47 E-value: 9.36e-05
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Name | Accession | Description | Interval | E-value | ||||||
TctC | COG3181 | Tripartite-type tricarboxylate transporter, extracytoplasmic receptor component TctC [Energy ... |
1-320 | 3.90e-73 | ||||||
Tripartite-type tricarboxylate transporter, extracytoplasmic receptor component TctC [Energy production and conversion]; Pssm-ID: 442414 Cd Length: 324 Bit Score: 228.49 E-value: 3.90e-73
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PBP2_Bug_TTT | cd07012 | Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains ... |
31-317 | 1.14e-68 | ||||||
Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains the type 2 periplasmic binding fold; The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) proteins present in a number of bacterial species, but mainly in proteobacteria. In eubacteria, at least three families of periplasmic binding-protein dependent transporters are known: the ATP-binding cassette (ABC) transporters, the tripartite ATP-independent periplasmic transporters, and the tripartite tricarboxylate transporters (TTT). Bug proteins are the PBP components of the TTT. Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter. Pssm-ID: 270234 Cd Length: 291 Bit Score: 215.80 E-value: 1.14e-68
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PBP2_Bug27 | cd13578 | Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the ... |
31-310 | 1.39e-36 | ||||||
Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold; Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity. Pssm-ID: 270296 Cd Length: 291 Bit Score: 132.63 E-value: 1.39e-36
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PBP2_Bug_NagM | cd13579 | Uncharacterized NagM-like protein of Bug (Bordetella uptake gene) protein family; contains the ... |
31-310 | 1.16e-25 | ||||||
Uncharacterized NagM-like protein of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold; The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter. Pssm-ID: 270297 Cd Length: 292 Bit Score: 103.51 E-value: 1.16e-25
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PBP2_BugD_Asp | cd13576 | Aspartic acid transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 ... |
32-280 | 2.46e-25 | ||||||
Aspartic acid transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold; The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter. Pssm-ID: 270294 Cd Length: 294 Bit Score: 102.83 E-value: 2.46e-25
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PBP2_BugE_Glu | cd13577 | Glutamate transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 ... |
31-317 | 8.06e-25 | ||||||
Glutamate transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold; The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter. Pssm-ID: 270295 Cd Length: 292 Bit Score: 101.27 E-value: 8.06e-25
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TctC | pfam03401 | Tripartite tricarboxylate transporter family receptor; These probable extra-cytoplasmic solute ... |
47-320 | 3.78e-22 | ||||||
Tripartite tricarboxylate transporter family receptor; These probable extra-cytoplasmic solute receptors are strongly overrepresented in several beta-proteobacteria. This family, formerly known as Bug - Bordetella uptake gene (bug) product - is a family of bacterial tripartite tricarboxylate receptors of the extracytoplasmic solute binding receptor-dependent transporter group of families, distinct from the ABC and TRAP-T families. The TctABC system has been characterized in S. typhimurium, and TctC is the extracytoplasmic tricarboxylate-binding receptor which binds the transporters TctA and TctB, two integral membrane proteins. Complete three-component systems are found only in bacteria. Pssm-ID: 397461 Cd Length: 274 Bit Score: 93.70 E-value: 3.78e-22
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PBP2_PhnD_like | cd01071 | Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ... |
126-230 | 4.15e-07 | ||||||
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: 50.34 E-value: 4.15e-07
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PhnD | COG3221 | ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ... |
109-299 | 6.53e-07 | ||||||
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 442454 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 6.53e-07
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TauA | COG0715 | ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ... |
68-224 | 1.25e-06 | ||||||
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 440479 [Multi-domain] Cd Length: 297 Bit Score: 49.23 E-value: 1.25e-06
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Imp | COG2358 | TRAP-type uncharacterized transport system, periplasmic component [General function prediction ... |
18-237 | 4.57e-06 | ||||||
TRAP-type uncharacterized transport system, periplasmic component [General function prediction only]; Pssm-ID: 441925 [Multi-domain] Cd Length: 303 Bit Score: 47.53 E-value: 4.57e-06
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Phosphonate-bd | pfam12974 | ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ... |
109-299 | 5.01e-06 | ||||||
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: 46.87 E-value: 5.01e-06
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TRAP_TAXI | TIGR02122 | TRAP transporter solute receptor, TAXI family; This family is one of at least three major ... |
1-230 | 9.36e-05 | ||||||
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: 43.47 E-value: 9.36e-05
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PBP2_Atu4678_like | cd13696 | The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ... |
125-255 | 2.44e-04 | ||||||
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: 41.59 E-value: 2.44e-04
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PBP2_ThiY | cd13651 | Substrate binding domain of ABC-type transporters for thiamin biosynthetic pathway ... |
127-213 | 3.13e-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: 41.19 E-value: 3.13e-04
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NMT1 | pfam09084 | NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed ... |
117-213 | 4.04e-04 | ||||||
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: 41.05 E-value: 4.04e-04
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PBP2_SsuA_like_5 | cd13562 | Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ... |
87-205 | 5.84e-04 | ||||||
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: 40.56 E-value: 5.84e-04
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PBP2_TAXI_TRAP | cd13520 | Substrate binding domain of TAXI proteins of the tripartite ATP-independent periplasmic ... |
112-203 | 1.04e-03 | ||||||
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: 40.29 E-value: 1.04e-03
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Blast search parameters | ||||
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