phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators
Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Comment:also 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
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