ABC transporter substrate-binding protein [Thermococcus gorgonarius]
Protein Classification
PBP2_NikA_DppA_OppA_like and CGP_CTERM domain-containing protein( domain architecture ID 11973317)
protein containing domains COG3889, PBP2_NikA_DppA_OppA_like, and CGP_CTERM
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| COG3889 super family | cl28569 | Extracellular solute-binding protein, contains Ig-fold domain [General function prediction ... |
375-769 | 1.90e-64 | |||||||
Extracellular solute-binding protein, contains Ig-fold domain [General function prediction only]; The actual alignment was detected with superfamily member COG3889: Pssm-ID: 443097 [Multi-domain] Cd Length: 878 Bit Score: 232.23 E-value: 1.90e-64
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| COG3889 super family | cl28569 | Extracellular solute-binding protein, contains Ig-fold domain [General function prediction ... |
24-347 | 7.56e-50 | |||||||
Extracellular solute-binding protein, contains Ig-fold domain [General function prediction only]; The actual alignment was detected with superfamily member COG3889: Pssm-ID: 443097 [Multi-domain] Cd Length: 878 Bit Score: 189.47 E-value: 7.56e-50
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| CGP_CTERM | TIGR04288 | CGP-CTERM domain; This domain has an essentially invariant motif, Cys-Gly-Pro, followed by a ... |
804-823 | 5.68e-07 | |||||||
CGP-CTERM domain; This domain has an essentially invariant motif, Cys-Gly-Pro, followed by a highly hydrophobic transmembrane domain, always at the protein C-terminus. It occurs, so far, strictly in the family Thermococcaceae (includes Thermococcus and Pyrococcus) within the Euryarchaeota. It occurs in ten proteins per genome on average, and proteins with the domain may lack similarity elsewhere. The presumed sorting/processing protein, for which this domain contains the recognition sequence, is unknown, but it is unlikely to be a member of the exosortase/archaeosortase family. The Cys residue suggests a lipid modification. Upstream, from this domain, most member proteins have an extremely Thr-rich sequence, suggesting archaeal surface protein O-linked glycosylation. : Pssm-ID: 213901 Cd Length: 20 Bit Score: 46.20 E-value: 5.68e-07
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| Name | Accession | Description | Interval | E-value | |||||||
| COG3889 | COG3889 | Extracellular solute-binding protein, contains Ig-fold domain [General function prediction ... |
375-769 | 1.90e-64 | |||||||
Extracellular solute-binding protein, contains Ig-fold domain [General function prediction only]; Pssm-ID: 443097 [Multi-domain] Cd Length: 878 Bit Score: 232.23 E-value: 1.90e-64
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| COG3889 | COG3889 | Extracellular solute-binding protein, contains Ig-fold domain [General function prediction ... |
24-347 | 7.56e-50 | |||||||
Extracellular solute-binding protein, contains Ig-fold domain [General function prediction only]; Pssm-ID: 443097 [Multi-domain] Cd Length: 878 Bit Score: 189.47 E-value: 7.56e-50
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| SBP_bac_5 | pfam00496 | Bacterial extracellular solute-binding proteins, family 5 Middle; The borders of this family ... |
317-622 | 5.07e-10 | |||||||
Bacterial extracellular solute-binding proteins, family 5 Middle; The borders of this family are based on the PDBSum definitions of the domain edges for Swiss:P06202. Pssm-ID: 425718 Cd Length: 368 Bit Score: 62.04 E-value: 5.07e-10
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| PBP2_NikA_DppA_OppA_like | cd00995 | The substrate-binding domain of an ABC-type nickel/oligopeptide-like import system contains ... |
321-709 | 5.98e-08 | |||||||
The substrate-binding domain of an ABC-type nickel/oligopeptide-like import system contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain of nickel/dipeptide/oligopeptide transport systems, which function in the import of nickel and peptides, and other closely related proteins. The oligopeptide-binding protein OppA is a periplasmic component of an ATP-binding cassette (ABC) transport system OppABCDEF consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Similar to the ABC-type dipeptide and oligopeptide import systems, nickel transporter is comprised of five subunits NikABCDE: the two pore-forming integral inner membrane proteins NikB and NikC; the two inner membrane-associated proteins with ATPase activity NikD and NikE; and the periplasmic nickel binding NikA, which is the initial nickel receptor that controls the chemotactic response away from nickel. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand binding domains of ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173853 [Multi-domain] Cd Length: 466 Bit Score: 56.16 E-value: 5.98e-08
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| CGP_CTERM | TIGR04288 | CGP-CTERM domain; This domain has an essentially invariant motif, Cys-Gly-Pro, followed by a ... |
804-823 | 5.68e-07 | |||||||
CGP-CTERM domain; This domain has an essentially invariant motif, Cys-Gly-Pro, followed by a highly hydrophobic transmembrane domain, always at the protein C-terminus. It occurs, so far, strictly in the family Thermococcaceae (includes Thermococcus and Pyrococcus) within the Euryarchaeota. It occurs in ten proteins per genome on average, and proteins with the domain may lack similarity elsewhere. The presumed sorting/processing protein, for which this domain contains the recognition sequence, is unknown, but it is unlikely to be a member of the exosortase/archaeosortase family. The Cys residue suggests a lipid modification. Upstream, from this domain, most member proteins have an extremely Thr-rich sequence, suggesting archaeal surface protein O-linked glycosylation. Pssm-ID: 213901 Cd Length: 20 Bit Score: 46.20 E-value: 5.68e-07
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| Name | Accession | Description | Interval | E-value | |||||||
| COG3889 | COG3889 | Extracellular solute-binding protein, contains Ig-fold domain [General function prediction ... |
375-769 | 1.90e-64 | |||||||
Extracellular solute-binding protein, contains Ig-fold domain [General function prediction only]; Pssm-ID: 443097 [Multi-domain] Cd Length: 878 Bit Score: 232.23 E-value: 1.90e-64
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| COG3889 | COG3889 | Extracellular solute-binding protein, contains Ig-fold domain [General function prediction ... |
24-347 | 7.56e-50 | |||||||
Extracellular solute-binding protein, contains Ig-fold domain [General function prediction only]; Pssm-ID: 443097 [Multi-domain] Cd Length: 878 Bit Score: 189.47 E-value: 7.56e-50
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| DdpA | COG0747 | ABC-type transport system, periplasmic component [Amino acid transport and metabolism]; |
318-723 | 3.03e-11 | |||||||
ABC-type transport system, periplasmic component [Amino acid transport and metabolism]; Pssm-ID: 440510 [Multi-domain] Cd Length: 464 Bit Score: 66.49 E-value: 3.03e-11
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| SBP_bac_5 | pfam00496 | Bacterial extracellular solute-binding proteins, family 5 Middle; The borders of this family ... |
317-622 | 5.07e-10 | |||||||
Bacterial extracellular solute-binding proteins, family 5 Middle; The borders of this family are based on the PDBSum definitions of the domain edges for Swiss:P06202. Pssm-ID: 425718 Cd Length: 368 Bit Score: 62.04 E-value: 5.07e-10
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| PBP2_NikA_DppA_OppA_like | cd00995 | The substrate-binding domain of an ABC-type nickel/oligopeptide-like import system contains ... |
321-709 | 5.98e-08 | |||||||
The substrate-binding domain of an ABC-type nickel/oligopeptide-like import system contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain of nickel/dipeptide/oligopeptide transport systems, which function in the import of nickel and peptides, and other closely related proteins. The oligopeptide-binding protein OppA is a periplasmic component of an ATP-binding cassette (ABC) transport system OppABCDEF consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Similar to the ABC-type dipeptide and oligopeptide import systems, nickel transporter is comprised of five subunits NikABCDE: the two pore-forming integral inner membrane proteins NikB and NikC; the two inner membrane-associated proteins with ATPase activity NikD and NikE; and the periplasmic nickel binding NikA, which is the initial nickel receptor that controls the chemotactic response away from nickel. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand binding domains of ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173853 [Multi-domain] Cd Length: 466 Bit Score: 56.16 E-value: 5.98e-08
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| CGP_CTERM | TIGR04288 | CGP-CTERM domain; This domain has an essentially invariant motif, Cys-Gly-Pro, followed by a ... |
804-823 | 5.68e-07 | |||||||
CGP-CTERM domain; This domain has an essentially invariant motif, Cys-Gly-Pro, followed by a highly hydrophobic transmembrane domain, always at the protein C-terminus. It occurs, so far, strictly in the family Thermococcaceae (includes Thermococcus and Pyrococcus) within the Euryarchaeota. It occurs in ten proteins per genome on average, and proteins with the domain may lack similarity elsewhere. The presumed sorting/processing protein, for which this domain contains the recognition sequence, is unknown, but it is unlikely to be a member of the exosortase/archaeosortase family. The Cys residue suggests a lipid modification. Upstream, from this domain, most member proteins have an extremely Thr-rich sequence, suggesting archaeal surface protein O-linked glycosylation. Pssm-ID: 213901 Cd Length: 20 Bit Score: 46.20 E-value: 5.68e-07
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| PBP2_TmCBP_oligosaccharides_like | cd08509 | The substrate binding domain of a cellulose-binding protein from Thermotoga maritima contains ... |
321-718 | 8.96e-07 | |||||||
The substrate binding domain of a cellulose-binding protein from Thermotoga maritima contains the type 2 periplasmic binding fold; This family represents the substrate-binding domain of a cellulose-binding protein from the hyperthermophilic bacterium Thermotoga maritima (TmCBP) and its closest related proteins. TmCBP binds a variety of lengths of beta-1,4-linked glucose oligomers, ranging from two sugar rings (cellobiose) to five (cellopentose). TmCBP is structurally homologous to domains I and III of the ATP-binding cassette (ABC)-type oligopeptide-binding proteins and thus belongs to the type 2 periplasmic binding fold protein (PBP2) superfamily. The type 2 periplasmic binding proteins are soluble ligand-binding components of ABC or tripartite ATP-independent transporters and chemotaxis systems. Members of the PBP2 superfamily function in uptake of a variety of metabolites in bacteria such as amino acids, carbohydrate, ions, and polyamines. Ligands are then transported across the cytoplasmic membrane energized by ATP hydrolysis or electrochemical ion gradient. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173874 [Multi-domain] Cd Length: 509 Bit Score: 52.32 E-value: 8.96e-07
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| PBP2_NikA_DppA_OppA_like_4 | cd08500 | The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide ... |
321-590 | 1.18e-05 | |||||||
The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold; This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173865 [Multi-domain] Cd Length: 499 Bit Score: 48.78 E-value: 1.18e-05
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| PBP2_AppA_like | cd08514 | The substrate-binding component of the oligopeptide-binding protein, AppA, from Bacillus ... |
321-639 | 3.83e-05 | |||||||
The substrate-binding component of the oligopeptide-binding protein, AppA, from Bacillus subtilis contains the type 2 periplasmic-binding fold; This family represents the substrate-binding domain of the oligopeptide-binding protein, AppA, from Bacillus subtilis and its closest homologs from other bacteria and archaea. Bacillus subtilis has three ABC-type peptide transport systems, a dipeptide-binding protein (DppA) and two oligopeptide-binding proteins (OppA and AppA) with overlapping specificity. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and also is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173879 [Multi-domain] Cd Length: 483 Bit Score: 47.23 E-value: 3.83e-05
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| PBP2_clavulanate_OppA2 | cd08506 | The substrate-binding domain of an oligopeptide binding protein (OppA2) from the biosynthesis ... |
318-628 | 8.20e-05 | |||||||
The substrate-binding domain of an oligopeptide binding protein (OppA2) from the biosynthesis pathway of the beta-lactamase inhibitor clavulanic acid contains the type 2 periplasmic binding fold; Clavulanic acid (CA), a clinically important beta-lactamase inhibitor, is one of a family of clavams produced as secondary metabolites by fermentation of Streptomyces clavuligeru. The biosynthesis of CA proceeds via multiple steps from the precursors, glyceraldehyde-3-phosphate and arginine. CA possesses a characteristic (3R,5R) stereochemistry essential for reaction with penicillin-binding proteins and beta-lactamases. Two genes (oppA1 and oppA2) in the clavulanic acid gene cluster encode oligopeptide-binding proteins that are required for CA biosynthesis. OppA1/2 is involved in the binding and transport of peptides across the cell membrane of Streptomyces clavuligerus. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173871 [Multi-domain] Cd Length: 466 Bit Score: 46.10 E-value: 8.20e-05
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| PBP2_OppA | cd08504 | The substrate-binding component of an ABC-type oligopetide import system contains the type 2 ... |
324-530 | 1.27e-04 | |||||||
The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173869 [Multi-domain] Cd Length: 498 Bit Score: 45.24 E-value: 1.27e-04
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| OppA | COG4166 | ABC-type oligopeptide transport system, periplasmic component [Amino acid transport and ... |
324-529 | 5.19e-04 | |||||||
ABC-type oligopeptide transport system, periplasmic component [Amino acid transport and metabolism]; Pssm-ID: 443327 [Multi-domain] Cd Length: 543 Bit Score: 43.66 E-value: 5.19e-04
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| PBP2_NikA_DppA_OppA_like_3 | cd08490 | The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide ... |
455-590 | 1.46e-03 | |||||||
The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold; This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173855 [Multi-domain] Cd Length: 470 Bit Score: 41.82 E-value: 1.46e-03
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| PBP2_NikA_DppA_OppA_like_11 | cd08516 | The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide ... |
311-493 | 2.32e-03 | |||||||
The substrate-binding component of an uncharacterized ABC-type nickel/dipeptide/oligopeptide-like import system contains the type 2 periplasmic binding fold; This CD represents the substrate-binding domain of an uncharacterized ATP-binding cassette (ABC) type nickel/dipeptide/oligopeptide-like transporter. The oligopeptide-binding protein OppA and the dipeptide-binding protein DppA show significant sequence similarity to NikA, the initial nickel receptor. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173881 [Multi-domain] Cd Length: 457 Bit Score: 41.47 E-value: 2.32e-03
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