thiamine ABC transporter substrate binding subunit [Glaesserella parasuis]
Protein Classification
thiamine ABC transporter substrate binding subunit( domain architecture ID 10008329)
thiamine ABC transporter substrate binding subunit functions as the primary receptor for the active transport of thiamine (vitamin B1) in an ATP-dependent manner; belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| TbpA | COG4143 | ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ... |
1-326 | 8.55e-149 | ||||||
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism]; : Pssm-ID: 443315 [Multi-domain] Cd Length: 343 Bit Score: 421.95 E-value: 8.55e-149
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| Name | Accession | Description | Interval | E-value | ||||||
| TbpA | COG4143 | ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ... |
1-326 | 8.55e-149 | ||||||
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism]; Pssm-ID: 443315 [Multi-domain] Cd Length: 343 Bit Score: 421.95 E-value: 8.55e-149
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| thiB | TIGR01276 | thiamine ABC transporter, periplasmic binding protein; This model finds the thiamine (and ... |
21-326 | 6.39e-144 | ||||||
thiamine ABC transporter, periplasmic binding protein; This model finds the thiamine (and thiamine pyrophosphate) ABC transporter periplasmic binding protein ThiB in proteobacteria. Completed genomes having this protein (E. coli, Vibrio cholera, Haemophilus influenzae) also have the permease ThiP, described by TIGRFAMs equivalog model TIGR01253. [Transport and binding proteins, Other] Pssm-ID: 130343 Cd Length: 309 Bit Score: 408.26 E-value: 6.39e-144
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| PBP2_TbpA | cd13545 | Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ... |
23-287 | 5.86e-97 | ||||||
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-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: 270263 [Multi-domain] Cd Length: 269 Bit Score: 287.66 E-value: 5.86e-97
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| SBP_bac_11 | pfam13531 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
25-276 | 8.56e-11 | ||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 60.74 E-value: 8.56e-11
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| PRK15046 | PRK15046 | 2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
5-189 | 2.08e-07 | ||||||
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 52.00 E-value: 2.08e-07
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| Name | Accession | Description | Interval | E-value | ||||||
| TbpA | COG4143 | ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ... |
1-326 | 8.55e-149 | ||||||
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism]; Pssm-ID: 443315 [Multi-domain] Cd Length: 343 Bit Score: 421.95 E-value: 8.55e-149
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| thiB | TIGR01276 | thiamine ABC transporter, periplasmic binding protein; This model finds the thiamine (and ... |
21-326 | 6.39e-144 | ||||||
thiamine ABC transporter, periplasmic binding protein; This model finds the thiamine (and thiamine pyrophosphate) ABC transporter periplasmic binding protein ThiB in proteobacteria. Completed genomes having this protein (E. coli, Vibrio cholera, Haemophilus influenzae) also have the permease ThiP, described by TIGRFAMs equivalog model TIGR01253. [Transport and binding proteins, Other] Pssm-ID: 130343 Cd Length: 309 Bit Score: 408.26 E-value: 6.39e-144
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| sfuA | TIGR01254 | ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC ... |
21-320 | 2.06e-129 | ||||||
ABC transporter periplasmic binding protein, thiB subfamily; The model describes thiamine ABC transporter, periplasmic protein in bacteria and archae. The protein belongs to the larger ABC transport system. It consists of at least three components: the thiamine binding periplasmic protein; an inner membrane permease; an ATP-binding subunit. It has been experimentally demonstrated that the mutants in the various steps in the de novo synthesis of the thiamine and the biologically active form, namely thiamine pyrophosphate can be exogenously supplemented with thiamine, thiamine monophosphate (TMP) or thiamine pyrophosphate (TPP). [Transport and binding proteins, Other] Pssm-ID: 130321 [Multi-domain] Cd Length: 304 Bit Score: 371.50 E-value: 2.06e-129
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| PBP2_TbpA | cd13545 | Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ... |
23-287 | 5.86e-97 | ||||||
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-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: 270263 [Multi-domain] Cd Length: 269 Bit Score: 287.66 E-value: 5.86e-97
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| PBP2_Fe3_thiamine_like | cd13518 | Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
23-284 | 7.79e-37 | ||||||
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 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: 270236 [Multi-domain] Cd Length: 260 Bit Score: 132.81 E-value: 7.79e-37
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| AfuA | COG1840 | ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
46-324 | 5.53e-26 | ||||||
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 104.63 E-value: 5.53e-26
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| PotD | COG0687 | Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
5-326 | 4.98e-25 | ||||||
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 103.07 E-value: 4.98e-25
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| PBP2_BitB | cd13546 | Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
23-276 | 2.17e-13 | ||||||
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-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: 270264 [Multi-domain] Cd Length: 258 Bit Score: 68.82 E-value: 2.17e-13
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| ModA | COG0725 | ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ... |
5-279 | 2.18e-12 | ||||||
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440489 [Multi-domain] Cd Length: 253 Bit Score: 66.05 E-value: 2.18e-12
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| PBP2_polyamine_RpCGA009 | cd13589 | The periplasmic-binding component of an uncharacterized ABC transport system from ... |
23-273 | 1.94e-11 | ||||||
The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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: 270307 [Multi-domain] Cd Length: 268 Bit Score: 63.40 E-value: 1.94e-11
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| PBP2_Fbp_like_1 | cd13544 | Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
23-292 | 3.37e-11 | ||||||
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-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: 270262 [Multi-domain] Cd Length: 292 Bit Score: 63.00 E-value: 3.37e-11
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| SBP_bac_11 | pfam13531 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
25-276 | 8.56e-11 | ||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 60.74 E-value: 8.56e-11
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| SBP_bac_1 | pfam01547 | Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
53-273 | 3.88e-09 | ||||||
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF. Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 56.66 E-value: 3.88e-09
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| PBP2_PotD_PotF_like | cd13590 | The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
23-277 | 8.38e-09 | ||||||
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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: 270308 [Multi-domain] Cd Length: 315 Bit Score: 56.09 E-value: 8.38e-09
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| PRK15046 | PRK15046 | 2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
5-189 | 2.08e-07 | ||||||
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 52.00 E-value: 2.08e-07
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| MalE | COG2182 | Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-293 | 2.53e-07 | ||||||
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 51.87 E-value: 2.53e-07
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| SBP_bac_6 | pfam13343 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
77-305 | 3.66e-07 | ||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 50.44 E-value: 3.66e-07
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| SBP_bac_8 | pfam13416 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
127-294 | 2.35e-06 | ||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 48.17 E-value: 2.35e-06
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| PBP2_polyamine_1 | cd13588 | The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
46-274 | 3.86e-06 | ||||||
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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: 270306 [Multi-domain] Cd Length: 279 Bit Score: 47.68 E-value: 3.86e-06
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| PBP2_polyamines | cd13523 | The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
23-277 | 3.97e-06 | ||||||
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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: 270241 [Multi-domain] Cd Length: 268 Bit Score: 47.43 E-value: 3.97e-06
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| PBP2_AEPn_like | cd13548 | Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ... |
24-196 | 5.00e-06 | ||||||
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-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: 270266 [Multi-domain] Cd Length: 310 Bit Score: 47.56 E-value: 5.00e-06
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| PBP2_Fbp_like_6 | cd13552 | Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
46-277 | 5.40e-05 | ||||||
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-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: 270270 [Multi-domain] Cd Length: 266 Bit Score: 43.98 E-value: 5.40e-05
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| PBP2_Maltodextrin | cd13657 | The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
112-186 | 1.90e-04 | ||||||
The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270375 [Multi-domain] Cd Length: 368 Bit Score: 42.75 E-value: 1.90e-04
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| PBP2_Fbp_like_4 | cd13550 | Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
67-285 | 9.57e-04 | ||||||
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-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: 270268 [Multi-domain] Cd Length: 265 Bit Score: 40.21 E-value: 9.57e-04
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| PBP2_Maltose_binding_like | cd13586 | The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
120-148 | 1.81e-03 | ||||||
The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270304 [Multi-domain] Cd Length: 367 Bit Score: 39.59 E-value: 1.81e-03
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| PBP2_TpPotD_like | cd13662 | The periplasmic substrate-binding component of an ABC-type polyamine transport system from ... |
120-303 | 2.60e-03 | ||||||
The periplasmic substrate-binding component of an ABC-type polyamine transport system from Treponema pallidum and related proteins; contains the type 2 periplasmic binding fold; This group includes the polyamine-binding component of an ABC-type polyamine transport system from Treponema pallidum and closely related proteins, which is homologous to the spermidine-preferring periplasmic substrate-binding protein component (PotD)of ABC transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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: 270380 Cd Length: 312 Bit Score: 39.04 E-value: 2.60e-03
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| PBP2_AvModA | cd13539 | Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the ... |
176-279 | 3.71e-03 | ||||||
Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate is where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA 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: 270257 [Multi-domain] Cd Length: 226 Bit Score: 38.32 E-value: 3.71e-03
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| PBP2_Fbp | cd13543 | Substrate binding domain of ferric iron transporter, a member of the type 2 periplasmic ... |
240-287 | 9.85e-03 | ||||||
Substrate binding domain of ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic protein (Fbp) has high affinities for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-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: 270261 [Multi-domain] Cd Length: 306 Bit Score: 37.28 E-value: 9.85e-03
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