MULTISPECIES: ABC transporter substrate-binding protein [Enterococcus]
Protein Classification
ABC transporter substrate-binding protein( domain architecture ID 11447308)
ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| UgpB | COG1653 | ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-336 | 1.93e-65 | ||||||
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism]; : Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 213.37 E-value: 1.93e-65
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| Name | Accession | Description | Interval | E-value | ||||||
| UgpB | COG1653 | ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-336 | 1.93e-65 | ||||||
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism]; Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 213.37 E-value: 1.93e-65
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| PBP2_TMBP_like | cd13585 | The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
36-414 | 4.93e-61 | ||||||
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. 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: 270303 [Multi-domain] Cd Length: 383 Bit Score: 202.25 E-value: 4.93e-61
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| SBP_bac_1 | pfam01547 | Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
50-331 | 6.60e-31 | ||||||
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: 120.21 E-value: 6.60e-31
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| Name | Accession | Description | Interval | E-value | |||||||
| UgpB | COG1653 | ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1-336 | 1.93e-65 | |||||||
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism]; Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 213.37 E-value: 1.93e-65
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| PBP2_TMBP_like | cd13585 | The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
36-414 | 4.93e-61 | |||||||
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. 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: 270303 [Multi-domain] Cd Length: 383 Bit Score: 202.25 E-value: 4.93e-61
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| PBP2_UgpB | cd14748 | The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
36-414 | 2.81e-44 | |||||||
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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: 270451 [Multi-domain] Cd Length: 385 Bit Score: 158.22 E-value: 2.81e-44
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| MalE | COG2182 | Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1-417 | 1.65e-40 | |||||||
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 148.94 E-value: 1.65e-40
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| PBP2_XBP1_like | cd14749 | The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
36-341 | 1.60e-36 | |||||||
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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: 270452 [Multi-domain] Cd Length: 388 Bit Score: 137.51 E-value: 1.60e-36
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| PBP2_MalE | cd14747 | Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
38-344 | 2.00e-32 | |||||||
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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: 270450 [Multi-domain] Cd Length: 386 Bit Score: 126.27 E-value: 2.00e-32
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| PBP2_TMBP | cd14750 | The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
51-414 | 3.64e-32 | |||||||
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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: 270453 [Multi-domain] Cd Length: 385 Bit Score: 125.48 E-value: 3.64e-32
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| SBP_bac_1 | pfam01547 | Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
50-331 | 6.60e-31 | |||||||
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: 120.21 E-value: 6.60e-31
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| SBP_bac_8 | pfam13416 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
52-341 | 3.27e-26 | |||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 106.72 E-value: 3.27e-26
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| PBP2_Maltose_binding_like | cd13586 | The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
36-349 | 1.58e-25 | |||||||
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: 106.61 E-value: 1.58e-25
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| PBP2_GacH | cd14751 | The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
41-412 | 9.82e-25 | |||||||
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are 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: 270454 [Multi-domain] Cd Length: 376 Bit Score: 104.38 E-value: 9.82e-25
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| PBP2_ABC_oligosaccharides | cd13522 | The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
38-413 | 7.60e-22 | |||||||
The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, 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: 270240 [Multi-domain] Cd Length: 368 Bit Score: 95.94 E-value: 7.60e-22
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| PBP2_AlgQ_like_1 | cd13580 | Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
36-333 | 1.15e-20 | |||||||
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide. Pssm-ID: 270298 [Multi-domain] Cd Length: 471 Bit Score: 93.55 E-value: 1.15e-20
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| PBP2_CMBP | cd13658 | The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
56-333 | 3.46e-19 | |||||||
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. 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: 270376 [Multi-domain] Cd Length: 372 Bit Score: 88.31 E-value: 3.46e-19
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| PBP2_Maltodextrin | cd13657 | The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
50-334 | 1.17e-16 | |||||||
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: 80.88 E-value: 1.17e-16
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| PBP2_AlgQ_like | cd13521 | Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
58-377 | 2.81e-15 | |||||||
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide. Pssm-ID: 270239 [Multi-domain] Cd Length: 483 Bit Score: 77.50 E-value: 2.81e-15
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| PBP2_AlgQ_like_4 | cd13583 | Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
41-179 | 1.28e-13 | |||||||
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide. Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 72.39 E-value: 1.28e-13
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| PotD | COG0687 | Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
5-334 | 1.55e-13 | |||||||
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 71.10 E-value: 1.55e-13
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| PBP2_polyamine_RpCGA009 | cd13589 | The periplasmic-binding component of an uncharacterized ABC transport system from ... |
36-334 | 2.01e-12 | |||||||
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: 66.87 E-value: 2.01e-12
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| AfuA | COG1840 | ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
53-345 | 9.06e-12 | |||||||
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 65.34 E-value: 9.06e-12
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| PBP2_AlgQ_like_2 | cd13581 | Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
36-272 | 3.77e-10 | |||||||
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide. Pssm-ID: 270299 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 3.77e-10
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| PBP2_FutA1_ilke | cd13542 | Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic ... |
51-336 | 8.64e-08 | |||||||
Substrate binding domain of ferric iron-binding protein, a member of the type 2 periplasmic binding fold superfamily; FutA1 is the periplasmic component of an ABC-type iron transporter and serves as the primary receptor in Synerchosystis species. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria and is critical for survival of these pathogens within the host. After binding iron with high affinity, FutA1 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: 270260 [Multi-domain] Cd Length: 314 Bit Score: 53.49 E-value: 8.64e-08
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| PBP2_AlgQ_like_3 | cd13582 | Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
45-333 | 2.31e-06 | |||||||
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 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. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide. Pssm-ID: 270300 [Multi-domain] Cd Length: 504 Bit Score: 49.63 E-value: 2.31e-06
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| PBP2_Fe3_thiamine_like | cd13518 | Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
36-336 | 5.16e-06 | |||||||
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: 47.68 E-value: 5.16e-06
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| PBP2_polyamine_1 | cd13588 | The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
56-172 | 7.32e-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: 47.29 E-value: 7.32e-06
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| PBP2_ModA_WtpA | cd13540 | Substrate binding domain of ModA/WtpA from Pyrococcus furiosus and its closest homologs;the ... |
286-338 | 6.28e-04 | |||||||
Substrate binding domain of ModA/WtpA from Pyrococcus furiosus 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 where the central metal atom is in a hexacoordinate configuration. 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: 270258 [Multi-domain] Cd Length: 263 Bit Score: 41.13 E-value: 6.28e-04
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| PBP2_Fbp_like_2 | cd13547 | Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
51-340 | 6.57e-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: 270265 [Multi-domain] Cd Length: 259 Bit Score: 41.05 E-value: 6.57e-04
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| SBP_bac_6 | pfam13343 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
134-337 | 8.07e-04 | |||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 40.81 E-value: 8.07e-04
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| PBP2_ModA_like_1 | cd13538 | Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ... |
306-337 | 1.96e-03 | |||||||
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. 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. 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: 270256 [Multi-domain] Cd Length: 230 Bit Score: 39.59 E-value: 1.96e-03
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| TupB | COG2998 | ABC-type tungstate transport system, permease component TupA [Inorganic ion transport and ... |
1-68 | 2.27e-03 | |||||||
ABC-type tungstate transport system, permease component TupA [Inorganic ion transport and metabolism]; Pssm-ID: 442236 Cd Length: 272 Bit Score: 39.38 E-value: 2.27e-03
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| PBP2_oligosaccharide_1 | cd13655 | The periplasmic binding component of ABC tansport system specific for an unknown ... |
124-341 | 5.22e-03 | |||||||
The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. 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: 270373 [Multi-domain] Cd Length: 363 Bit Score: 38.87 E-value: 5.22e-03
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| PBP2_PotD_PotF_like | cd13590 | The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
36-159 | 5.81e-03 | |||||||
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: 38.37 E-value: 5.81e-03
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| PBP2_Fbp_like_1 | cd13544 | Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
304-354 | 8.11e-03 | |||||||
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: 37.97 E-value: 8.11e-03
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