| Primary Identifier | IPR024181 | Type | Family |
| Short Name | Chemotax_regulator_CheV |
| description | This group contains chemotaxis response regulator protein CheV. 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.In bacterial chemotaxis, cellular movement is directed in response to chemical gradients. Transmembrane chemoreceptors that sense the stimuli are coupled (via a 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). In CheA, a histidine protein kinase domain is fused to the amino-terminus of the SH3 region [, ]. 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 []and the CheV proteins play a role in the bacterial mobility [].For additional information please see []. |
