phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR
Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. 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: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.",