phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins
This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Feature 1: metal binding site [ion binding site], 3 residue positions
Conserved feature residue pattern:[ED] [ED] [ED]
Evidence:
Comment:based on metal binding site of other family members
Comment:signal transduction in two-component systems is mediated by metal ion dependent phosphorelay reactions between protein histidine kinases and phosphoaccepting receiver domains in response regulator proteins
Comment:for many receivers, Mg2+ is the preferred metal ion, but other divalent ions such as Mn2+ are also used
Jiyao W et al.(2023). "The conserved domain database in 2023.",