UniProt functional annotation for P0ACQ4

UniProt code: P0ACQ4.

Organism: Escherichia coli (strain K12).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
 
Function: Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto- aggregation ability. {ECO:0000269|PubMed:9497290}.
 
Activity regulation: Activated by oxidation of Cys-199 resulting in the alternative formation of cystine, sulfenic acid, S-nitroso- or glutathione-bound cysteine.
Subunit: Homodimer and homotetramer.
Ptm: Oxidized on Cys-199; the Cys-SOH formed in response to oxidative signaling triggers a conformational change and the onset of transcriptional activity with a specific DNA-binding affinity. Cys-199- SOH rapidly reacts with Cys-208-SH to form a disulfide bond. {ECO:0000269|PubMed:12015987}.
Ptm: S-nitrosylation in response to nitrosative signaling triggers a conformational change and the onset of transcriptional activity with a specific DNA-binding affinity. {ECO:0000269|PubMed:12015987}.
Ptm: Glutathionylation in response to redox signaling triggers the onset of transcriptional activity with a specific DNA-binding affinity. {ECO:0000269|PubMed:12015987}.
Miscellaneous: Oxidized OxyR can be reduced and inactivated by glutaredoxin 1, the product of grxA, whose expression is regulated by OxyR itself.
Miscellaneous: Identified as a multicopy suppressor of the slow growth phenotype of an rsgA (yjeQ) deletion mutant. {ECO:0000269|PubMed:18223068}.
Similarity: Belongs to the LysR transcriptional regulatory family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.