Protein Domain : Chemotaxis protein-glutamate methylesterase IPR011247

Type	Family
Description	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. Phosphorylated CheY binds to FliM, a component of the flagellar motor switch complex, and modulates the direction of flagellar rotation [ ]. Response regulator CheB (receptor modification enzyme, protein-glutamate methylesterase) modulates the signalling output of the chemotaxis receptors through control of the level of chemoreceptor methylation []. Specific glutamyl residues in the transmembrane chemoreceptor cytoplasmic domain are methylated by methyltransferase CheR to form γ-carboxyl glutamyl methyl esters. These esters can be hydrolyzed by methylesterase CheB. Receptor modification resets the signalling states of receptors, allowing for responses to changes in concentration of the chemical stimuli irrespective of their absolute concentrations [].Proteins in this family contain a divergent form of the CheB-like protein-glutamate methylesterase domain in the C-terminal region. This domain is usually found fused with the CheY-like receiver (response regulator) domain, forming CheB response regulator methylesterase ( ). The stand-alone form is presumed also to be involved in the process of regulating bacterial chemotaxis [ ], but there is no experimental evidence to confirm this.
Short Name	Chemotax_prot-Glu_Me-esterase