Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
218-541
4.18e-106
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 PRK15041:
Pssm-ID: 481250 [Multi-domain] Cd Length: 554 Bit Score: 329.99 E-value: 4.18e-106
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
50-186
1.69e-10
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.
:
Pssm-ID: 438629 [Multi-domain] Cd Length: 138 Bit Score: 59.19 E-value: 1.69e-10
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
273-520
1.23e-62
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: 207.14 E-value: 1.23e-62
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
300-491
1.77e-50
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: 172.81 E-value: 1.77e-50
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
331-488
8.60e-48
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: 164.53 E-value: 8.60e-48
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
50-186
1.69e-10
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.
Pssm-ID: 438629 [Multi-domain] Cd Length: 138 Bit Score: 59.19 E-value: 1.69e-10
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
5-190
9.06e-04
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 40.70 E-value: 9.06e-04
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
273-520
1.23e-62
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: 207.14 E-value: 1.23e-62
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
300-491
1.77e-50
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: 172.81 E-value: 1.77e-50
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
331-488
8.60e-48
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: 164.53 E-value: 8.60e-48
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar ...
50-186
1.69e-10
ligand-binding sensor domain of Comamonas testosteroni CNB-2 MCP2201 and similar chemoreceptors; This family includes the ligand-binding sensor domain of Comamonas testosteroni transmembrane chemoreceptor CNB-2 MCP2201 and similar chemoreceptors. The C. testosteroni methyl-accepting chemotaxis protein MCP2201 triggers chemotaxis towards tricarboxylic acid cycle intermediates such as citric acid and aromatic compounds. While the apo-form ligand binding domain (LBD) forms a typical four-helix bundle homodimer, similar to other chemoreceptors in the superfamily such as Escherichia coli Tar and Tsr, the citrate-bound LBD reveals a four-helix bundle homotrimer. This type of oligomerization has never been observed in other bacterial chemoreceptor LBD. Site-directed mutations of key amino acid residues have demonstrated the physiological importance of the homotrimer for chemotaxis.
Pssm-ID: 438629 [Multi-domain] Cd Length: 138 Bit Score: 59.19 E-value: 1.69e-10
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
248-350
2.98e-04
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: 42.66 E-value: 2.98e-04
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
5-190
9.06e-04
Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors. This domain recognizes citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 432749 [Multi-domain] Cd Length: 181 Bit Score: 40.70 E-value: 9.06e-04
Tape measure protein; This entry represents phage tape measure proteins that are required to ...
304-476
1.45e-03
Tape measure protein; This entry represents phage tape measure proteins that are required to assemble the page tail. The protein serves as a base for tail tube protein polymerization and acts as a template for tail length determination.
Pssm-ID: 466312 [Multi-domain] Cd Length: 192 Bit Score: 39.90 E-value: 1.45e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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