CheW

Two component signalling adaptor domain
CheW
SMART accession number:SM00260
Description: -
Interpro abstract (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)].

GO process:chemotaxis (GO:0006935), signal transduction (GO:0007165)
Family alignment:
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There are 55999 CheW domains in 53950 proteins in SMART's nrdb database.

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