ID   OXYR_ECOL6              Reviewed;         305 AA.
AC   P0ACQ5; P11721; P22471;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Hydrogen peroxide-inducible genes activator;
DE   AltName: Full=Morphology and auto-aggregation control protein;
GN   Name=oxyR; OrderedLocusNames=c4922;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Hydrogen peroxide sensor. Activates the expression of a
CC       regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC,
CC       ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is
CC       negatively autoregulated by binding to a 43 bp region upstream of its
CC       own coding sequence. OxyR is inactivated by reduction of its essential
CC       disulfide bond by the product of GrxA, itself positively regulated by
CC       OxyR. Has also a positive regulatory effect on the production of
CC       surface proteins that control the colony morphology and auto-
CC       aggregation ability (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Activated by oxidation of Cys-199 resulting in the
CC       alternative formation of cystine, sulfenic acid, S-nitroso- or
CC       glutathione-bound cysteine. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000250}.
CC   -!- PTM: Oxidized on Cys-199; the Cys-SOH formed in response to oxidative
CC       signaling triggers a conformational change and the onset of
CC       transcriptional activity with a specific DNA-binding affinity. Cys-199-
CC       SOH rapidly reacts with Cys-208-SH to form a disulfide bond (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: S-nitrosylation in response to nitrosative signaling triggers a
CC       conformational change and the onset of transcriptional activity with a
CC       specific DNA-binding affinity. {ECO:0000250}.
CC   -!- PTM: Glutathionylation in response to redox signaling triggers the
CC       onset of transcriptional activity with a specific DNA-binding affinity.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Oxidized OxyR can be reduced and inactivated by
CC       glutaredoxin 1, the product of grxA, whose expression is regulated by
CC       OxyR itself. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83350.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83350.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001025939.1; NC_004431.1.
DR   AlphaFoldDB; P0ACQ5; -.
DR   SMR; P0ACQ5; -.
DR   STRING; 199310.c4922; -.
DR   PRIDE; P0ACQ5; -.
DR   EnsemblBacteria; AAN83350; AAN83350; c4922.
DR   GeneID; 66672127; -.
DR   KEGG; ecc:c4922; -.
DR   eggNOG; COG0583; Bacteria.
DR   HOGENOM; CLU_039613_6_4_6; -.
DR   OMA; DQALDIC; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   3: Inferred from homology;
KW   Activator; Disulfide bond; DNA-binding; Glutathionylation; Oxidation;
KW   S-nitrosylation; Transcription; Transcription regulation.
FT   CHAIN           1..305
FT                   /note="Hydrogen peroxide-inducible genes activator"
FT                   /id="PRO_0000105730"
FT   DOMAIN          1..58
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        18..37
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   MOD_RES         199
FT                   /note="Cysteine sulfenic acid (-SOH); alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         199
FT                   /note="S-glutathionyl cysteine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         199
FT                   /note="S-nitrosocysteine; alternate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        180..259
FT                   /evidence="ECO:0000250"
FT   DISULFID        199..208
FT                   /note="Alternate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  34276 MW;  714EF4169CED2EC9 CRC64;
     MNIRDLEYLV ALAEHRHFRR AADSCHVSQP TLSGQIRKLE DELGVMLLER TSRKVLFTQA
     GMLLVDQART VLREVKVLKE MASQQGETMS GPLHIGLIPT VGPYLLPHII PMLHQTFPKL
     EMYLHEAQTH QLLAQLDSGK LDCVILALVK ESEAFIEVPL FDEPMLLAIY EDHPWANREC
     VPMADLAGEK LLMLEDGHCL RDQAMGFCFE AGADEDTHFR ATSLETLRNM VAAGSGITLL
     PALAVPPERK RDGVVYLPCI KPEPRRTIGL VYRPGSPLRS RYEQLAEAIR ARMDGHFDKV
     LKQAV