Protein Domain : IPR012071

Type:  Family Name:  Chemotaxis glutamate methyltransferase
Description:  Members of this group contain a divergent form of CheB-like protein-glutamate methylesterase domain in the C-terminal region. This domain is usually found fused with CheY-like receiver (response regulator) domain, forming CheB response regulator methylesterase (). The stand-alone form () is presumed to be involved in the same process of regulating bacterial chemotaxis [], but there is no experimental evidence to confirm this. Members of this family have an N-terminal domain which has some amino acid residues in common with the CheY-like receiver domain but it is not clear whether it is evolutionarily or functionally related to CheY.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 gamma-carboxyl glutamyl methyl esters. These esters can be hydrolysed 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 [].For more information on CheB, please see and . Short Name:  Chemotax_glutamate_MeTrfase

0 Child Features

1 Contains

DB identifier Type Name
IPR000673 Domain Signal transduction response regulator, chemotaxis, protein-glutamate methylesterase

1 Cross References

Identifier
PIRSF036592

0 Found In

0 GO Annotation

0 Ontology Annotations

0 Parent Features

0 Proteins

2 Publications

First Author Title Year Journal Volume Pages PubMed ID
            10049806
            11912013