OXYR_ECOLI
ID OXYR_ECOLI Reviewed; 305 AA.
AC P0ACQ4; P11721; P22471; Q2M8Q6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Hydrogen peroxide-inducible genes activator;
DE AltName: Full=Morphology and auto-aggregation control protein;
GN Name=oxyR; Synonyms=momR, mor; OrderedLocusNames=b3961, JW3933;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2471187; DOI=10.1073/pnas.86.10.3484;
RA Christman M.F., Storz G., Ames B.N.;
RT "OxyR, a positive regulator of hydrogen peroxide-inducible genes in
RT Escherichia coli and Salmonella typhimurium, is homologous to a family of
RT bacterial regulatory proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3484-3488(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2551682; DOI=10.1002/j.1460-2075.1989.tb08370.x;
RA Boelker M., Kahmann R.;
RT "The Escherichia coli regulatory protein OxyR discriminates between
RT methylated and unmethylated states of the phage Mu mom promoter.";
RL EMBO J. 8:2403-2410(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2511419; DOI=10.1007/bf00332397;
RA Tao K., Makino K., Yonei S., Nakata A., Shinagawa H.;
RT "Molecular cloning and nucleotide sequencing of oxyR, the positive
RT regulatory gene of a regulon for an adaptive response to oxidative stress
RT in Escherichia coli: homologies between OxyR protein and a family of
RT bacterial activator proteins.";
RL Mol. Gen. Genet. 218:371-376(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2167922; DOI=10.1099/00221287-136-3-455;
RA Warne S.R., Varley J.M., Boulnois G.J., Norton M.G.;
RT "Identification and characterization of a gene that controls colony
RT morphology and auto-aggregation in Escherichia coli K12.";
RL J. Gen. Microbiol. 136:455-462(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP PROTEIN SEQUENCE OF 1-10.
RX PubMed=1864839;
RA Tao K., Makino K., Yonei S., Nakata A., Shinagawa H.;
RT "Purification and characterization of the Escherichia coli OxyR protein,
RT the positive regulator for a hydrogen peroxide-inducible regulon.";
RL J. Biochem. 109:262-266(1991).
RN [9]
RP FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-199 AND CYS-208.
RX PubMed=9497290; DOI=10.1126/science.279.5357.1718;
RA Zheng M., Aslund F., Storz G.;
RT "Activation of the OxyR transcription factor by reversible disulfide bond
RT formation.";
RL Science 279:1718-1721(1998).
RN [10]
RP S-NITROSYLATION AT CYS-199, GLUTATHIONYLATION AT CYS-199, OXIDATION AT
RP CYS-199, AND DISULFIDE BOND 180-CYS--CYS-259.
RX PubMed=12015987; DOI=10.1016/s0092-8674(02)00723-7;
RA Kim S.O., Merchant K., Nudelman R., Beyer W.F. Jr., Keng T., de Angelo J.,
RA Hausladen A., Stamler J.S.;
RT "OxyR: a molecular code for redox-related signaling.";
RL Cell 109:383-396(2002).
RN [11]
RP PARTIALLY SUPPRESSES AN RSGA MUTANT.
RC STRAIN=K12;
RX PubMed=18223068; DOI=10.1128/jb.01744-07;
RA Campbell T.L., Brown E.D.;
RT "Genetic interaction screens with ordered overexpression and deletion clone
RT sets implicate the Escherichia coli GTPase YjeQ in late ribosome
RT biogenesis.";
RL J. Bacteriol. 190:2537-2545(2008).
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. {ECO:0000269|PubMed:9497290}.
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.
CC -!- SUBUNIT: Homodimer and homotetramer.
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.
CC {ECO:0000269|PubMed:12015987}.
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:0000269|PubMed:12015987}.
CC -!- PTM: Glutathionylation in response to redox signaling triggers the
CC onset of transcriptional activity with a specific DNA-binding affinity.
CC {ECO:0000269|PubMed:12015987}.
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.
CC -!- MISCELLANEOUS: Identified as a multicopy suppressor of the slow growth
CC phenotype of an rsgA (yjeQ) deletion mutant.
CC {ECO:0000269|PubMed:18223068}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; J04553; AAA24257.1; -; Genomic_DNA.
DR EMBL; X52666; CAA36893.1; -; Genomic_DNA.
DR EMBL; X16531; CAA34534.1; -; Genomic_DNA.
DR EMBL; M34102; AAA24176.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43067.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76943.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77350.1; -; Genomic_DNA.
DR PIR; D65203; RGECOX.
DR RefSeq; NP_418396.1; NC_000913.3.
DR RefSeq; WP_001025939.1; NZ_STEB01000037.1.
DR PDB; 1I69; X-ray; 2.70 A; A/B=87-305.
DR PDB; 1I6A; X-ray; 2.30 A; A=87-305.
DR PDBsum; 1I69; -.
DR PDBsum; 1I6A; -.
DR AlphaFoldDB; P0ACQ4; -.
DR SMR; P0ACQ4; -.
DR BioGRID; 4263457; 17.
DR DIP; DIP-10419N; -.
DR IntAct; P0ACQ4; 2.
DR STRING; 511145.b3961; -.
DR jPOST; P0ACQ4; -.
DR PaxDb; P0ACQ4; -.
DR PRIDE; P0ACQ4; -.
DR EnsemblBacteria; AAC76943; AAC76943; b3961.
DR EnsemblBacteria; BAE77350; BAE77350; BAE77350.
DR GeneID; 66672127; -.
DR GeneID; 948462; -.
DR KEGG; ecj:JW3933; -.
DR KEGG; eco:b3961; -.
DR PATRIC; fig|1411691.4.peg.2744; -.
DR EchoBASE; EB0675; -.
DR eggNOG; COG0583; Bacteria.
DR HOGENOM; CLU_039613_6_4_6; -.
DR InParanoid; P0ACQ4; -.
DR OMA; DQALDIC; -.
DR PhylomeDB; P0ACQ4; -.
DR BioCyc; EcoCyc:PD00214; -.
DR BioCyc; MetaCyc:PD00214; -.
DR EvolutionaryTrace; P0ACQ4; -.
DR PRO; PR:P0ACQ4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0051409; P:response to nitrosative stress; IDA:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Direct protein sequencing; Disulfide bond;
KW DNA-binding; Glutathionylation; Oxidation; Reference proteome;
KW S-nitrosylation; Transcription; Transcription regulation.
FT CHAIN 1..305
FT /note="Hydrogen peroxide-inducible genes activator"
FT /id="PRO_0000105728"
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:0000269|PubMed:12015987"
FT MOD_RES 199
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:12015987"
FT MOD_RES 199
FT /note="S-nitrosocysteine; alternate"
FT /evidence="ECO:0000269|PubMed:12015987"
FT DISULFID 180..259
FT /evidence="ECO:0000269|PubMed:12015987"
FT DISULFID 199..208
FT /note="Alternate"
FT /evidence="ECO:0000269|PubMed:9497290"
FT MUTAGEN 199
FT /note="C->S,A: No activation following redox signaling."
FT /evidence="ECO:0000269|PubMed:9497290"
FT MUTAGEN 208
FT /note="C->S,A: No activation following redox signaling."
FT /evidence="ECO:0000269|PubMed:9497290"
FT CONFLICT 154
FT /note="A -> R (in Ref. 2; AAA24257)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="R -> A (in Ref. 4; AAA24176)"
FT /evidence="ECO:0000305"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1I6A"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 155..170
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1I6A"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1I69"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1I6A"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1I6A"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:1I6A"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:1I6A"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:1I6A"
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
