Protein Domain : Chemotaxis protein CheW IPR039315

Type	Family
Description	In bacterial chemotaxis, cellular movement is directed in response to chemical gradients. Transmembrane chemoreceptors that sense the stimuli are coupled via coupling protein CheW with a signal transduction histidine kinase (CheA) [ , ]. CheA phosphorylates response regulators CheB and CheY. The two cytoplasmic proteins, CheW and CheA, both contain homologous SH3-like domains that interact with transmembrane chemoreceptors, or methyl accepting chemotaxis proteins (MCPs). CheV is a third type of protein with a CheW-like domain.In Bacillus subtilis, CheW and CheV may be partially redundant in coupling the receptors to CheA; however, they are both necessary for efficient chemotaxis [ ]. CheV is phosphorylated in vitro on a conserved aspartate as a result of phosphoryl group transfer from phosphorylated CheA (CheA-P). This reaction is slower compared with the phospho-transfer reaction between CheA-P and one other response regulator of the system, CheB. It is part of a signal transduction pathway to facilitate adaptation to attractants []. In Helicobacter pylori, CheV paralogues and CheW are not redundant and seem to have separate roles in chemotaxis []. CheV is a two-domain protein with an N-terminal CheW-like (SH3-like) domain and a C-terminal CheY-like receiver domain. It is often regarded as a version of CheW, where the CheW-like domain is fused to the receiver domain [].This group contains chemotaxis response regulator proteins CheW.
Short Name	CheW