InterPro : IPR008248

Name  Signal transduction response regulator, chemotaxis, CheB Short Name  Sig_transdc_resp-reg_CheB
Type  Family Description  Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions []. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk []. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more []. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) []. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK.A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [, ].This entry represents response regulators involved in chemoreceptor modification. 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 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 [].Response regulators of the microbial two-component signal transduction systems typically consist of an N-terminal CheY-like receiver domain and a C-terminal output (usually DNA-binding) domain [,]. In members of this group, the output domain is an enzymatic domain, protein-glutamate methylesterase (demethylase, ). In response to an environmental stimulus, a phosphoryl group is transferred from the His residue of a signal transduction histidine kinase to an Asp residue in the CheY-like receiver domain of the cognate response regulator. Phosphorylation of the receiver domain induces conformational changes that activate an associated output domain. Phosphorylation-induced conformational changes in the response regulator molecule have been demonstrated in direct structural studies []. In members of this group, phosphorylation of receiver domain activates the methylesterase [], resulting in the subsequent demethylation of the chemoreceptors.For additional information please see [, , , , ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

2 Contains

Id Name Short Name Type
IPR001789 Signal transduction response regulator, receiver domain Sig_transdc_resp-reg_receiver Domain
IPR000673 Signal transduction response regulator, chemotaxis, protein-glutamate methylesterase Sig_transdc_resp-reg_Me-estase Domain

0 Found In

0 Parent Features

15 Publications

First Author Title Year Journal Volume Pages
Wolanin PM Histidine protein kinases: key signal transducers outside the animal kingdom. 2002 Genome Biol 3 REVIEWS3013
Stock AM Two-component signal transduction. 2000 Annu Rev Biochem 69 183-215
Skerker JM Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. 2005 PLoS Biol 3 e334
Laub MT Specificity in two-component signal transduction pathways. 2007 Annu Rev Genet 41 121-45
Varughese KI Molecular recognition of bacterial phosphorelay proteins. 2002 Curr Opin Microbiol 5 142-8
Hoch JA Keeping signals straight in phosphorelay signal transduction. 2001 J Bacteriol 183 4941-9
West AH Histidine kinases and response regulator proteins in two-component signaling systems. 2001 Trends Biochem Sci 26 369-76
Lewis RJ Dimer formation and transcription activation in the sporulation response regulator Spo0A. 2002 J Mol Biol 316 235-45
Volz K Structural conservation in the CheY superfamily. 1993 Biochemistry 32 11741-53
Djordjevic S Structural analysis of bacterial chemotaxis proteins: components of a dynamic signaling system. 1998 J Struct Biol 124 189-200
Lupas A Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis. 1989 J Biol Chem 264 17337-42
Falke JJ The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes. 1997 Annu Rev Cell Dev Biol 13 457-512
Anand GS Activation of methylesterase CheB: evidence of a dual role for the regulatory domain. 1998 Biochemistry 37 14038-47
Barnakov AN Allosteric enhancement of adaptational demethylation by a carboxyl-terminal sequence on chemoreceptors. 2002 J Biol Chem 277 42151-6
Jurica MS Mind your B's and R's: bacterial chemotaxis, signal transduction and protein recognition. 1998 Structure 6 809-13

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)