Protein Domain : CheW-like domain IPR002545

Type	Domain
Description	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, whichmonitors the environmental conditions and its substrate, the response regulator, which acts as a binary switch depending on the phosphorylationstate. In Escherichia coli, the signal transduction pathway for chemotaxis consists of specialised membrane receptors, termed chemotaxis transducers; aCheA-CheY two-component system, which transmits the signal from transducers to flagellar motors; and a docking protein, CheW, which couples the CheAhistidine kinase to transducers. Whereas CheW is only made of a CheW-like domain, CheA additionally contains an HPt domain and anhistidine kinase domain. The CheW-like domain has been shown to mediate the interaction between CheA and the adaptor protein CheW. Somebacteria 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, CheVprobably acts in adaptation to attractants [ , , , ].The CheW-like domain is composed of two β-sheet subdomains, each of which forms a loose five-stranded β-barrel around an internal hydrophobic core. The interactions between the subdomains are contributed by athird hydrophobic core sandwiched between the two β-sheet subdomains. The CheW-like structure is stabilised by extensive hydrophobic interactions [, ].
Short Name	CheW-lke_dom