MULTISPECIES: TRAP transporter substrate-binding protein [Enterobacteriaceae]
Protein Classification
TRAP transporter substrate-binding protein( domain architecture ID 10194660)
TRAP transporter substrate-binding protein functions as the receptor subunit of a Tripartite ATP-independent Periplasmic (TRAP) transporter complex, similar to Salmonella enterica uncharacterized protein YiiZ
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PBP2_TRAP_SBP_like_3 | cd13671 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
25-320 | 2.20e-144 | |||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. : Pssm-ID: 270389 [Multi-domain] Cd Length: 296 Bit Score: 408.87 E-value: 2.20e-144
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| Name | Accession | Description | Interval | E-value | ||||||
| PBP2_TRAP_SBP_like_3 | cd13671 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
25-320 | 2.20e-144 | ||||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270389 [Multi-domain] Cd Length: 296 Bit Score: 408.87 E-value: 2.20e-144
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| DctP | COG1638 | TRAP-type C4-dicarboxylate transport system, periplasmic component [Carbohydrate transport and ... |
1-323 | 4.43e-116 | ||||||
TRAP-type C4-dicarboxylate transport system, periplasmic component [Carbohydrate transport and metabolism]; Pssm-ID: 441245 [Multi-domain] Cd Length: 329 Bit Score: 338.35 E-value: 4.43e-116
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| DctP | pfam03480 | Bacterial extracellular solute-binding protein, family 7; This family of proteins is involved ... |
28-308 | 2.75e-93 | ||||||
Bacterial extracellular solute-binding protein, family 7; This family of proteins is involved in binding extracellular solutes for transport across the bacterial cytoplasmic membrane. This family includes Swiss:P37735, a C4-dicarboxylate-binding protein and the sialic acid-binding protein SiaP. The structure of the SiaP receptor has revealed an overall topology similar to ATP binding cassette ESR (extracytoplasmic solute receptors) proteins. Upon binding of sialic acid, SiaP undergoes domain closure about a hinge region and kinking of an alpha-helix hinge component. Pssm-ID: 427325 [Multi-domain] Cd Length: 286 Bit Score: 278.75 E-value: 2.75e-93
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| TRAP_S1 | NF037995 | TRAP transporter substrate-binding protein DctP; Proteins of this family are members of the ... |
27-294 | 5.20e-82 | ||||||
TRAP transporter substrate-binding protein DctP; Proteins of this family are members of the superfamily of Tripartite ATP-independent Periplasmic Transporter (TRAP-T). They transport hydrophobic substrates, usually lipoprotein. Pssm-ID: 468304 [Multi-domain] Cd Length: 271 Bit Score: 249.44 E-value: 5.20e-82
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| dctP | TIGR00787 | tripartite ATP-independent periplasmic transporter solute receptor, DctP family; TRAP-T ... |
28-283 | 1.48e-81 | ||||||
tripartite ATP-independent periplasmic transporter solute receptor, DctP family; TRAP-T (Tripartite ATP-independent Periplasmic Transporter) family proteins generally consist of three components, and these systems have so far been found in Gram-negative bacteria, Gram-postive bacteria and archaea. The best characterized example is the DctPQM system of Rhodobacter capsulatus, a C4 dicarboxylate (malate, fumarate, succinate) transporter. This model represents the DctP family, one of at least three major families of extracytoplasmic solute receptor for TRAP family transporters. Other are the SnoM family (see pfam03480) and TAXI (TRAP-associated extracytoplasmic immunogenic) family. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids] Pssm-ID: 129869 [Multi-domain] Cd Length: 257 Bit Score: 247.67 E-value: 1.48e-81
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| Name | Accession | Description | Interval | E-value | ||||||
| PBP2_TRAP_SBP_like_3 | cd13671 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
25-320 | 2.20e-144 | ||||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270389 [Multi-domain] Cd Length: 296 Bit Score: 408.87 E-value: 2.20e-144
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| DctP | COG1638 | TRAP-type C4-dicarboxylate transport system, periplasmic component [Carbohydrate transport and ... |
1-323 | 4.43e-116 | ||||||
TRAP-type C4-dicarboxylate transport system, periplasmic component [Carbohydrate transport and metabolism]; Pssm-ID: 441245 [Multi-domain] Cd Length: 329 Bit Score: 338.35 E-value: 4.43e-116
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| PBP2_TRAP_Siap_TeaA_like | cd13603 | Substrate-binding domain of a sialic acid binding Tripartite ATP-independent Periplasmic ... |
25-320 | 1.06e-108 | ||||||
Substrate-binding domain of a sialic acid binding Tripartite ATP-independent Periplasmic transport system (SiaP) and related proteins; the type 2 periplasmic-binding protein fold; This subfamily includes the periplasmic-binding component of TRAP transport systems such as SiaP (a sialic acid binding virulence factor), TeaA (an ectoine binding protein), and an uncharacterized TM0322 from hyperthermophilic bacterium Thermotoga maritima. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270321 [Multi-domain] Cd Length: 297 Bit Score: 318.32 E-value: 1.06e-108
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| DctP | pfam03480 | Bacterial extracellular solute-binding protein, family 7; This family of proteins is involved ... |
28-308 | 2.75e-93 | ||||||
Bacterial extracellular solute-binding protein, family 7; This family of proteins is involved in binding extracellular solutes for transport across the bacterial cytoplasmic membrane. This family includes Swiss:P37735, a C4-dicarboxylate-binding protein and the sialic acid-binding protein SiaP. The structure of the SiaP receptor has revealed an overall topology similar to ATP binding cassette ESR (extracytoplasmic solute receptors) proteins. Upon binding of sialic acid, SiaP undergoes domain closure about a hinge region and kinking of an alpha-helix hinge component. Pssm-ID: 427325 [Multi-domain] Cd Length: 286 Bit Score: 278.75 E-value: 2.75e-93
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| PBP2_TRAP_DctP2_like | cd13676 | Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP2 and ... |
25-307 | 1.43e-88 | ||||||
Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP2 and related proteins; the type 2 periplasmic-binding protein fold; This subgroup includes TRAP transporter DctP2 and its similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270394 [Multi-domain] Cd Length: 297 Bit Score: 267.17 E-value: 1.43e-88
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| TRAP_S1 | NF037995 | TRAP transporter substrate-binding protein DctP; Proteins of this family are members of the ... |
27-294 | 5.20e-82 | ||||||
TRAP transporter substrate-binding protein DctP; Proteins of this family are members of the superfamily of Tripartite ATP-independent Periplasmic Transporter (TRAP-T). They transport hydrophobic substrates, usually lipoprotein. Pssm-ID: 468304 [Multi-domain] Cd Length: 271 Bit Score: 249.44 E-value: 5.20e-82
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| dctP | TIGR00787 | tripartite ATP-independent periplasmic transporter solute receptor, DctP family; TRAP-T ... |
28-283 | 1.48e-81 | ||||||
tripartite ATP-independent periplasmic transporter solute receptor, DctP family; TRAP-T (Tripartite ATP-independent Periplasmic Transporter) family proteins generally consist of three components, and these systems have so far been found in Gram-negative bacteria, Gram-postive bacteria and archaea. The best characterized example is the DctPQM system of Rhodobacter capsulatus, a C4 dicarboxylate (malate, fumarate, succinate) transporter. This model represents the DctP family, one of at least three major families of extracytoplasmic solute receptor for TRAP family transporters. Other are the SnoM family (see pfam03480) and TAXI (TRAP-associated extracytoplasmic immunogenic) family. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids] Pssm-ID: 129869 [Multi-domain] Cd Length: 257 Bit Score: 247.67 E-value: 1.48e-81
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| PBP2_TRAP_SBP_like_5 | cd13675 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
25-308 | 8.27e-81 | ||||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270393 [Multi-domain] Cd Length: 296 Bit Score: 247.17 E-value: 8.27e-81
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| PBP2_TRAP_YiaO_like | cd13679 | Substrate-binding domain of 2,3-diketo-L-gulonate-binding Tripartite ATP-independent ... |
25-309 | 3.46e-78 | ||||||
Substrate-binding domain of 2,3-diketo-L-gulonate-binding Tripartite ATP-independent Periplasmic transport system and related proteins; the type 2 periplasmic-binding protein fold; This subfamily includes the solute receptor protein YiaO of TRAP transport system. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270397 [Multi-domain] Cd Length: 298 Bit Score: 240.57 E-value: 3.46e-78
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| PBP2_TRAP_Siap | cd13672 | Substrate-binding domain of a sialic acid binding Tripartite ATP-independent Periplasmic ... |
25-305 | 3.13e-75 | ||||||
Substrate-binding domain of a sialic acid binding Tripartite ATP-independent Periplasmic transport system (SiaP); the type 2 periplasmic-binding protein fold; This subfamily represents the periplasmic-binding component of TRAP transport system SiaP, a sialic acid binding virulence factor. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270390 [Multi-domain] Cd Length: 295 Bit Score: 232.91 E-value: 3.13e-75
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| PBP2_TRAP_TM0322_like | cd13669 | Periplasmic component of TRAP-type C4-dicarboxylate transport system TM0322 from Thermotoga ... |
25-305 | 2.83e-74 | ||||||
Periplasmic component of TRAP-type C4-dicarboxylate transport system TM0322 from Thermotoga maritima and similar proteins; the type 2 periplasmic binding protein fold; This subgroup includes the hyperthermophilic bacterium Thermotoga maritima TRAP-type C4-dicarboxylate transport system TM0322 and its closely related proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270387 [Multi-domain] Cd Length: 296 Bit Score: 230.53 E-value: 2.83e-74
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| PBP2_TRAP_DctP10 | cd13678 | Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP10; the ... |
25-307 | 4.88e-64 | ||||||
Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP10; the type 2 periplasmic-binding protein fold; This subgroup includes TRAP transporter DctP10 and its similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270396 [Multi-domain] Cd Length: 300 Bit Score: 204.44 E-value: 4.88e-64
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| PBP2_TRAP_SBP_like_1 | cd13674 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
25-306 | 3.77e-63 | ||||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270392 [Multi-domain] Cd Length: 299 Bit Score: 202.13 E-value: 3.77e-63
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| PBP2_TRAP_SBP_like_6 | cd13677 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
25-309 | 4.93e-58 | ||||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270395 [Multi-domain] Cd Length: 304 Bit Score: 189.04 E-value: 4.93e-58
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| PBP2_TRAP_SBP_like_4 | cd13680 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
25-323 | 3.31e-47 | ||||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270398 [Multi-domain] Cd Length: 300 Bit Score: 160.94 E-value: 3.31e-47
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| PBP2_TRAP_UehA_TeaA | cd13668 | Periplasmic substrate-binding component of osmoregulatory TRAP transporters TeaA and UehA; the ... |
45-307 | 1.09e-45 | ||||||
Periplasmic substrate-binding component of osmoregulatory TRAP transporters TeaA and UehA; the type 2 periplasmic-binding protein fold; This subfamily includes the periplasmic-binding component of the ectoine-specific TRAP transporters TeaA from Halomonas elongata and UehA from Ruegeria pomeroyi. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270386 [Multi-domain] Cd Length: 305 Bit Score: 157.04 E-value: 1.09e-45
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| PBP2_TRAP | cd13527 | Substrate-binding component of Tripartite ATP-independent Periplasmic transporters and ... |
25-311 | 1.43e-45 | ||||||
Substrate-binding component of Tripartite ATP-independent Periplasmic transporters and related proteins; contains the type 2 periplasmic-binding protein fold; This family represents the TRAP Transporters that are specific to various ligands, including sialic acid (N-acetyl neuraminic acid), glutamate, ectoine, xylulose, C4-dicarboxylates such as succinate, malate and fumarate, and keto acids such as pyruvate and alpha-ketobutyrate. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. This family also includes some eukaryotic homologs that have not been functionally characterized. TRAP transporters are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270245 [Multi-domain] Cd Length: 301 Bit Score: 156.81 E-value: 1.43e-45
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| PBP2_TRAP_SBP_like_2 | cd13673 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
25-292 | 7.32e-42 | ||||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes uncharacterized periplasmic substrate-binding proteins similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270391 [Multi-domain] Cd Length: 301 Bit Score: 147.02 E-value: 7.32e-42
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| PBP2_TRAP_BpDctp6_7 | cd13602 | Substrate-binding domain of a pyroglutamic acid binding DctP subfamily of the tripartite ... |
40-311 | 1.02e-35 | ||||||
Substrate-binding domain of a pyroglutamic acid binding DctP subfamily of the tripartite ATP-independent periplasmic transporters; contains the type 2 periplasmic binding protein fold; DctP6 and DctP7 groups of the TRAP transporters that involved in pyroglutamic acid transport. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270320 [Multi-domain] Cd Length: 300 Bit Score: 130.81 E-value: 1.02e-35
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| PBP2_TRAP_Tp0957_like | cd13670 | Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic ... |
37-292 | 1.19e-35 | ||||||
Uncharacterized substrate-binding protein of the Tripartite ATP-independent Periplasmic transporter family; the type 2 periplasmic-binding protein fold; This subfamily includes the putative periplasmic substrate-binding protein Tp0957 from Treponema pallidum, which is similar to TRAP transport systems such as SiaP (a sialic acid binding virulence factor) and TeaA (an ectoine binding protein). TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270388 [Multi-domain] Cd Length: 298 Bit Score: 130.40 E-value: 1.19e-35
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| PBP2_TRAP_DctP_like_2 | cd13605 | Substrate-binding component of uncharacterized Tripartite ATP-independent Periplasmic ... |
26-317 | 3.35e-35 | ||||||
Substrate-binding component of uncharacterized Tripartite ATP-independent Periplasmic transporter; the type 2 periplasmic-binding protein fold; This family represents the TRAP Transporters that are specific to various ligands, including sialic acid (N-acetyl neuraminic acid), glutamate, ectoine, xylulose, C4-dicarboxylates such as succinate, malate and fumarate, and keto acids such as pyruvate and alpha-ketobutyrate. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. This CD also included some eukaryotic homologs that have not been functionally characterized. TRAP transporters are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270323 [Multi-domain] Cd Length: 303 Bit Score: 129.41 E-value: 3.35e-35
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| PBP2_TRAP_Dctp3_4 | cd13665 | Periplasmic substrate-binding component of TRAP-type C4-dicarboxylate transport system DctP3 ... |
25-311 | 5.25e-34 | ||||||
Periplasmic substrate-binding component of TRAP-type C4-dicarboxylate transport system DctP3 and DctP4; the type 2 periplasmic-binding protein fold; This group includes uncharacterized DctP3 and DctP 4 subfamilies of TRAP Transporters specific to C4-dicarboxylates such as succinate, malate and fumarate. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. This CD also included some eukaryotic homologs that have not been functionally characterized. TRAP transporters are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270383 [Multi-domain] Cd Length: 302 Bit Score: 126.16 E-value: 5.25e-34
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| PBP2_TRAP_DctP_like_1 | cd13666 | Substrate-binding component of an uncharacterized TRAP-type C4-dicarboxylate transport system; ... |
34-313 | 2.26e-32 | ||||||
Substrate-binding component of an uncharacterized TRAP-type C4-dicarboxylate transport system; the type 2 periplasmic-binding protein fold; This group includes a DctP subfamily of TRAP Transporters specific to C4-dicarboxylates such as succinate, malate and fumarate. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. This CD also included some eukaryotic homologs that have not been functionally characterized. TRAP transporters are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270384 [Multi-domain] Cd Length: 303 Bit Score: 121.96 E-value: 2.26e-32
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| PBP2_TRAP_DctP1_3_4_like | cd13601 | Periplasmic substrate-binding component of uncharacterized TRAP-type C4-dicarboxylate ... |
25-292 | 1.40e-26 | ||||||
Periplasmic substrate-binding component of uncharacterized TRAP-type C4-dicarboxylate transporter subfamilies; the type 2 periplasmic-binding protein fold; This model includes uncharacterized DctP subfamilies of the TRAP Transporters. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270319 [Multi-domain] Cd Length: 302 Bit Score: 106.25 E-value: 1.40e-26
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| PBP2_TRAP_Dctp5_like | cd13684 | Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP5 and ... |
39-299 | 1.41e-24 | ||||||
Substrate-binding component of Tripartite ATP-independent Periplasmic transporter DctP5 and related proteins; the type 2 periplasmic-binding protein fold; This subgroup includes TRAP transporter DctP5 and its similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270402 [Multi-domain] Cd Length: 314 Bit Score: 101.25 E-value: 1.41e-24
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| PBP2_TRAP_ketoacid_lactate_like | cd13604 | Substrate-binding domain of an alpha-keto acid binding Tripartite ATP-independent Periplasmic ... |
34-310 | 2.03e-22 | ||||||
Substrate-binding domain of an alpha-keto acid binding Tripartite ATP-independent Periplasmic transporter and related proteins; the type 2 periplasmic-binding protein fold; This family constitutes TRAP transporters that bind to ketoacids such as pyruvate and alpha-ketobutyrate, xylulose, and other unknown ligands. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270322 [Multi-domain] Cd Length: 306 Bit Score: 94.95 E-value: 2.03e-22
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| PBP2_TRAP_DctP6_7 | cd13683 | Substrate-binding domain of Tripartite ATP-independent Periplasmic transporter DctP6 and DctP7; ... |
34-291 | 1.83e-21 | ||||||
Substrate-binding domain of Tripartite ATP-independent Periplasmic transporter DctP6 and DctP7; type 2 periplasmic-binding protein fold; This subgroup includes TRAP-type mannitol/chloroaromatic compound transport system (Dctp6) and similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process and a smaller membrane of unknown function. The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the PBP2 superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270401 [Multi-domain] Cd Length: 304 Bit Score: 92.36 E-value: 1.83e-21
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| FcbT1 | COG4663 | TRAP-type mannitol/chloroaromatic compound transport system, periplasmic component [Secondary ... |
39-321 | 6.63e-18 | ||||||
TRAP-type mannitol/chloroaromatic compound transport system, periplasmic component [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 443700 [Multi-domain] Cd Length: 356 Bit Score: 83.25 E-value: 6.63e-18
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| PBP2_TRAP_DctP1 | cd13667 | Periplasmic substrate-binding component of an uncharacterized TRAP-type C4-dicarboxylate ... |
139-316 | 4.95e-15 | ||||||
Periplasmic substrate-binding component of an uncharacterized TRAP-type C4-dicarboxylate transport system DctP1; contains the type 2 periplasmic-binding protein fold; This group includes an uncharacterized DctP1 subfamily of the TRAP Transporters. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270385 [Multi-domain] Cd Length: 295 Bit Score: 74.30 E-value: 4.95e-15
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| PBP2_TRAP_lactate | cd13681 | Substrate-binding component of a lactate binding Tripartite ATP-independent Periplasmic ... |
39-309 | 8.61e-13 | ||||||
Substrate-binding component of a lactate binding Tripartite ATP-independent Periplasmic transporter and related proteins; the type 2 periplasmic-binding protein fold; This subgroup includes a lactate binding TRAP transporter and its similar proteins. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270399 [Multi-domain] Cd Length: 311 Bit Score: 67.97 E-value: 8.61e-13
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| PBP2_TRAP_alpha-ketoacid | cd13682 | Substrate-binding component of an alpha-keto acid binding Tripartite ATP-independent ... |
43-264 | 2.17e-10 | ||||||
Substrate-binding component of an alpha-keto acid binding Tripartite ATP-independent Periplasmic transporter and related proteins; contains the type 2 periplasmic-binding protein fold; This subgroup includes TRAP transporters that bind to ketoacids such as pyruvate and alpha-ketobutyrate, xylulose, and other unknown ligands. TRAP transporters are a large family of solute transporters ubiquitously found in bacteria and archaea. They are comprised of a periplasmic substrate-binding protein (SBP; often called the P subunit) and two unequally sized integral membrane components: a large transmembrane subunit involved in the translocation process (the M subunit) and a smaller membrane of unknown function (the Q subunit). The driving force of TRAP transporters is provided by electrochemical ion gradients (either protons or sodium ions) across the cytoplasmic membrane, rather than ATP hydrolysis. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270400 [Multi-domain] Cd Length: 323 Bit Score: 60.83 E-value: 2.17e-10
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| NMT1 | pfam09084 | NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed ... |
151-266 | 7.66e-03 | ||||||
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: 37.20 E-value: 7.66e-03
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