Summary: CheW-like domain
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CheW-like domain Provide feedback
CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA [1] binds to CheW, suggesting that these domains can interact with each other.
Literature references
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Bilwes AM, Alex LA, Crane BR, Simon MI; , Cell 1999;96:131-141.: Structure of CheA, a signal-transducing histidine kinase. PUBMED:9989504 EPMC:9989504
External database links
SCOP: | 1b3q |
SMART: | CheW |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002545
The CheW-like domain is an around 150-residue domain that is found in proteins involved in the two-component signaling systems regulating bacterial chemotaxis. Two components systems are composed of a receptor kinase, which monitors the environmental conditions and its substrate, the response regulator, which acts as a binary switch depending on the phosphorylation state. In Escherichia coli, the signal transduction pathway for chemotaxis consists of specialised membrane receptors, termed chemotaxis transducers; a CheA-CheY two-component system, which transmits the signal from transducers to flagellar motors; and a docking protein, CheW, which couples the CheA histidine kinase to transducers. Whereas CheW is only made of a CheW-like domain, CheA additionally contains an HPt domain and an histidine kinase domain. The CheW-like domain has been shown to mediate the interaction between CheA and the adaptor protein CheW. Some bacteria contain another bifunctional protein, CheV, consisting of an N- terminal CheW-like domain and a C-terminal response regulatory domain. Although its precise function in chemotaxis is unknown, CheV probably acts in adaptation to attractants [PUBMED:9989504, PUBMED:11553614, PUBMED:12511501, PUBMED:11799399].
The CheW-like domain is composed of two beta-sheet subdomains, each of which forms a loose five-stranded beta-barrel around an internal hydrophobic core. The interactions between the subdomains are contributed by a third hydrophobic core sandwiched between the two beta-sheet subdomains. The CheW-like structure is stabilised by extensive hydrophobic interactions [PUBMED:9989504, PUBMED:11799399].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Biological process | signal transduction (GO:0007165) |
chemotaxis (GO:0006935) |
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, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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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 (216) |
Full (19043) |
Representative proteomes | UniProt (90392) |
NCBI (122363) |
Meta (656) |
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RP15 (2893) |
RP35 (9767) |
RP55 (19250) |
RP75 (33958) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (216) |
Full (19043) |
Representative proteomes | UniProt (90392) |
NCBI (122363) |
Meta (656) |
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RP15 (2893) |
RP35 (9767) |
RP55 (19250) |
RP75 (33958) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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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
Seed source: | Pfam-B_579 (release 4.1) |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 216 |
Number in full: | 19043 |
Average length of the domain: | 135.70 aa |
Average identity of full alignment: | 20 % |
Average coverage of the sequence by the domain: | 32.07 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 138 | ||||||||||||
Family (HMM) version: | 20 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
There are 6 interactions for this family. More...
CheW H-kinase_dim HATPase_c MCPsignal HATPase_c H-kinase_dimStructures
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 CheW domain has been found. There are 20 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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