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38  structures 3748  species 0  interactions 55646  sequences 873  architectures

Family: MCPsignal (PF00015)

Summary: Methyl-accepting chemotaxis protein (MCP) signalling domain

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This is the Wikipedia entry entitled "Methyl-accepting chemotaxis protein". More...

Methyl-accepting chemotaxis protein Edit Wikipedia article

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Methyl-accepting chemotaxis protein (MCP) signalling domain Provide feedback

This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.

Literature references

  1. Hanlon DW, Marquez-Magana LM, Carpenter PB, Chamberlin MJ, Ordal GW; , J Biol Chem 1992;267:12055-12060.: Sequence and characterization of Bacillus subtilis CheW. PUBMED:1601874 EPMC:1601874


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004089

Methyl-accepting chemotaxis proteins (MCPs) are a family of bacterial receptors that mediate chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behaviour [ PUBMED:16359703 ]. Environmental diversity gives rise to diversity in bacterial signalling receptors, and consequently there are many genes encoding MCPs [ PUBMED:17299051 ]. For example, there are four well-characterised MCPs found in Escherichia coli: Tar (taxis towards aspartate and maltose, away from nickel and cobalt), Tsr (taxis towards serine, away from leucine, indole and weak acids), Trg (taxis towards galactose and ribose) and Tap (taxis towards dipeptides).

MCPs share similar topology and signalling mechanisms. MCPs either bind ligands directly or interact with ligand-binding proteins, transducing the signal to downstream signalling proteins in the cytoplasm. MCPs undergo two covalent modifications: deamidation and reversible methylation at a number of glutamate residues. Attractants increase the level of methylation, while repellents decrease it. The methyl groups are added by the methyl-transferase cheR and are removed by the methylesterase cheB. Most MCPs are homodimers that contain the following organisation: an N-terminal signal sequence that acts as a transmembrane domain in the mature protein; a poorly-conserved periplasmic receptor (ligand-binding) domain; a second transmembrane domain; and a highly-conserved C-terminal cytoplasmic domain that interacts with downstream signalling components. The C-terminal domain contains the glycosylated glutamate residues.

This entry represents the signalling domain found in several methyl-accepting chemotaxis proteins. This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(9)
Full
(55646)
Representative proteomes UniProt
(297891)
RP15
(7045)
RP35
(27323)
RP55
(57728)
RP75
(108096)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(9)
Full
(55646)
Representative proteomes UniProt
(297891)
RP15
(7045)
RP35
(27323)
RP55
(57728)
RP75
(108096)
Alignment:
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Sequence:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(9)
Full
(55646)
Representative proteomes UniProt
(297891)
RP15
(7045)
RP35
(27323)
RP55
(57728)
RP75
(108096)
Raw Stockholm Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download    

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Blast MCP1_ECOLI/361-421
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Sonnhammer ELL
Number in seed: 9
Number in full: 55646
Average length of the domain: 168.70 aa
Average identity of full alignment: 31 %
Average coverage of the sequence by the domain: 29.68 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 34.6 34.6
Trusted cut-off 34.6 34.6
Noise cut-off 34.5 34.5
Model length: 172
Family (HMM) version: 24
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MCPsignal domain has been found. There are 38 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
C0SP89 View 3D Structure Click here
G3XD24 View 3D Structure Click here
G3XDA3 View 3D Structure Click here
O06477 View 3D Structure Click here
O07621 View 3D Structure Click here
O32239 View 3D Structure Click here
P02941 View 3D Structure Click here
P02942 View 3D Structure Click here
P05704 View 3D Structure Click here
P07017 View 3D Structure Click here
P07018 View 3D Structure Click here
P0C6D8 View 3D Structure Click here
P0DMI3 View 3D Structure Click here
P0DMI4 View 3D Structure Click here
P0DMI5 View 3D Structure Click here
P15492 View 3D Structure Click here
P35841 View 3D Structure Click here
P39209 View 3D Structure Click here
P39214 View 3D Structure Click here
P39215 View 3D Structure Click here
P39216 View 3D Structure Click here
P39217 View 3D Structure Click here
P42257 View 3D Structure Click here
P50466 View 3D Structure Click here
P54576 View 3D Structure Click here
P55439 View 3D Structure Click here
P55652 View 3D Structure Click here
Q00986 View 3D Structure Click here
Q02755 View 3D Structure Click here
Q02929 View 3D Structure Click here
Q0VTI9 View 3D Structure Click here
Q2W4T8 View 3D Structure Click here
Q2W8M7 View 3D Structure Click here
Q52877 View 3D Structure Click here
Q55445 View 3D Structure Click here
Q5UXM8 View 3D Structure Click here
Q5V5V4 View 3D Structure Click here
Q88D09 View 3D Structure Click here
Q88E10 View 3D Structure Click here
Q88IY8 View 3D Structure Click here