MCP four helix bundle domain-containing protein with a HAMP domain, binds sensor ligands and may function as a methyl-accepting chemotaxis protein (MCP), a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
196-401
3.34e-71
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
The actual alignment was detected with superfamily member PRK15048:
Pssm-ID: 481250 [Multi-domain] Cd Length: 553 Bit Score: 232.97 E-value: 3.34e-71
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ...
26-173
2.37e-07
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand binding sensor domain of chemoreceptors and related sensor histidine kinases forms homodimers and binds to ligands via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This family includes ligand binding sensor domain of several chemoreceptors, such as Escherichia coli Tar, Tsr, NarQ, NarX, Pseudomonas aeruginosa KinB, Rhodopseudomonas palustris histidine kinase HK9 chemoreceptors, Comamonas testosteroni CNB-2 MCP2201 and Anaeromyxobacter dehalogenans histidine kinase Adeh_2942, among others.
The actual alignment was detected with superfamily member pfam02203:
Pssm-ID: 444710 [Multi-domain] Cd Length: 152 Bit Score: 49.99 E-value: 2.37e-07
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
270-400
1.82e-36
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 133.57 E-value: 1.82e-36
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
296-400
1.92e-31
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 118.49 E-value: 1.92e-31
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
329-401
2.87e-23
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 95.58 E-value: 2.87e-23
Tar ligand binding domain homolog; This entry represents the ligand-binding domain found in a ...
26-173
2.37e-07
Tar ligand binding domain homolog; This entry represents the ligand-binding domain found in a number of methyl-accepting chemotaxis receptors, such as E.coli Tar (taxis to aspartate and repellents), which is a receptor for the attractant L-aspartate and also recognizes proteogenic amino acids, phthalic acid, Malic acid, 3,4-dihydroxymandelic acid, citrate, benzoate and derivatives, protocatechuate, vanillate, quinate, shikimate and dehydroshikimate (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426656 [Multi-domain] Cd Length: 152 Bit Score: 49.99 E-value: 2.37e-07
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
270-400
1.82e-36
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 133.57 E-value: 1.82e-36
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
296-400
1.92e-31
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.
Pssm-ID: 206779 [Multi-domain] Cd Length: 200 Bit Score: 118.49 E-value: 1.92e-31
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
329-401
2.87e-23
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.
Pssm-ID: 333767 [Multi-domain] Cd Length: 172 Bit Score: 95.58 E-value: 2.87e-23
Tar ligand binding domain homolog; This entry represents the ligand-binding domain found in a ...
26-173
2.37e-07
Tar ligand binding domain homolog; This entry represents the ligand-binding domain found in a number of methyl-accepting chemotaxis receptors, such as E.coli Tar (taxis to aspartate and repellents), which is a receptor for the attractant L-aspartate and also recognizes proteogenic amino acids, phthalic acid, Malic acid, 3,4-dihydroxymandelic acid, citrate, benzoate and derivatives, protocatechuate, vanillate, quinate, shikimate and dehydroshikimate (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426656 [Multi-domain] Cd Length: 152 Bit Score: 49.99 E-value: 2.37e-07
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.
Pssm-ID: 381743 [Multi-domain] Cd Length: 45 Bit Score: 40.89 E-value: 2.88e-05
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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