Pathways & interactions
CheW-like domain superfamily (IPR036061)
Short name: CheW-like_dom_sf
- CheW-like domain (IPR002545)
- Uncharacterised conserved protein UCP020479, signal transduction CheW-like (IPR014506)
- Chemotaxis response regulator CheV (IPR024181)
- Chemotaxis protein CheW/CheV (IPR039315)
This entry represents the CheW-like domain superfamily.
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 [PMID: 9989504, PMID: 11553614, PMID: 12511501, PMID: 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 [PMID: 9989504, PMID: 11799399].
- SSF50341 (SSF50341)