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Hydrogen peroxide-inducible genes activator (Morphology and auto-aggregation control protein)

 OXYR_ECOLI              Reviewed;         305 AA.
P0ACQ4; P11721; P22471; Q2M8Q6;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
22-NOV-2005, sequence version 1.
28-MAR-2018, entry version 104.
RecName: Full=Hydrogen peroxide-inducible genes activator;
AltName: Full=Morphology and auto-aggregation control protein;
Name=oxyR; Synonyms=momR, mor; OrderedLocusNames=b3961, JW3933;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2471187; DOI=10.1073/pnas.86.10.3484;
Christman M.F., Storz G., Ames B.N.;
"OxyR, a positive regulator of hydrogen peroxide-inducible genes in
Escherichia coli and Salmonella typhimurium, is homologous to a family
of bacterial regulatory proteins.";
Proc. Natl. Acad. Sci. U.S.A. 86:3484-3488(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2551682;
Boelker M., Kahmann R.;
"The Escherichia coli regulatory protein OxyR discriminates between
methylated and unmethylated states of the phage Mu mom promoter.";
EMBO J. 8:2403-2410(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2511419; DOI=10.1007/BF00332397;
Tao K., Makino K., Yonei S., Nakata A., Shinagawa H.;
"Molecular cloning and nucleotide sequencing of oxyR, the positive
regulatory gene of a regulon for an adaptive response to oxidative
stress in Escherichia coli: homologies between OxyR protein and a
family of bacterial activator proteins.";
Mol. Gen. Genet. 218:371-376(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2167922; DOI=10.1099/00221287-136-3-455;
Warne S.R., Varley J.M., Boulnois G.J., Norton M.G.;
"Identification and characterization of a gene that controls colony
morphology and auto-aggregation in Escherichia coli K12.";
J. Gen. Microbiol. 136:455-462(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8265357; DOI=10.1093/nar/21.23.5408;
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the
region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[8]
PROTEIN SEQUENCE OF 1-10.
PubMed=1864839;
Tao K., Makino K., Yonei S., Nakata A., Shinagawa H.;
"Purification and characterization of the Escherichia coli OxyR
protein, the positive regulator for a hydrogen peroxide-inducible
regulon.";
J. Biochem. 109:262-266(1991).
[9]
FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-199 AND CYS-208.
PubMed=9497290; DOI=10.1126/science.279.5357.1718;
Zheng M., Aslund F., Storz G.;
"Activation of the OxyR transcription factor by reversible disulfide
bond formation.";
Science 279:1718-1721(1998).
[10]
S-NITROSYLATION AT CYS-199, GLUTATHIONYLATION AT CYS-199, OXIDATION AT
CYS-199, AND DISULFIDE BOND 180-CYS--CYS-259.
PubMed=12015987; DOI=10.1016/S0092-8674(02)00723-7;
Kim S.O., Merchant K., Nudelman R., Beyer W.F. Jr., Keng T.,
de Angelo J., Hausladen A., Stamler J.S.;
"OxyR: a molecular code for redox-related signaling.";
Cell 109:383-396(2002).
-!- 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}.
-!- ENZYME 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.
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EMBL; J04553; AAA24257.1; -; Genomic_DNA.
EMBL; X52666; CAA36893.1; -; Genomic_DNA.
EMBL; X16531; CAA34534.1; -; Genomic_DNA.
EMBL; M34102; AAA24176.1; -; Genomic_DNA.
EMBL; U00006; AAC43067.1; -; Genomic_DNA.
EMBL; U00096; AAC76943.1; -; Genomic_DNA.
EMBL; AP009048; BAE77350.1; -; Genomic_DNA.
PIR; D65203; RGECOX.
RefSeq; NP_418396.1; NC_000913.3.
RefSeq; WP_001025939.1; NZ_LN832404.1.
PDB; 1I69; X-ray; 2.70 A; A/B=87-305.
PDB; 1I6A; X-ray; 2.30 A; A=87-305.
PDBsum; 1I69; -.
PDBsum; 1I6A; -.
ProteinModelPortal; P0ACQ4; -.
SMR; P0ACQ4; -.
BioGrid; 4263457; 17.
DIP; DIP-10419N; -.
IntAct; P0ACQ4; 2.
STRING; 316385.ECDH10B_4150; -.
DrugBank; DB03793; Benzoic Acid.
EPD; P0ACQ4; -.
PaxDb; P0ACQ4; -.
PRIDE; P0ACQ4; -.
EnsemblBacteria; AAC76943; AAC76943; b3961.
EnsemblBacteria; BAE77350; BAE77350; BAE77350.
GeneID; 948462; -.
KEGG; ecj:JW3933; -.
KEGG; eco:b3961; -.
PATRIC; fig|1411691.4.peg.2744; -.
EchoBASE; EB0675; -.
EcoGene; EG10681; oxyR.
eggNOG; ENOG4105C5Q; Bacteria.
eggNOG; ENOG410XNR2; LUCA.
HOGENOM; HOG000233514; -.
InParanoid; P0ACQ4; -.
KO; K04761; -.
OMA; YLMPRMI; -.
PhylomeDB; P0ACQ4; -.
BioCyc; EcoCyc:PD00214; -.
EvolutionaryTrace; P0ACQ4; -.
PRO; PR:P0ACQ4; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0000986; F:bacterial-type proximal promoter sequence-specific DNA binding; IDA:EcoCyc.
GO; GO:0001131; F:transcription factor activity, bacterial-type RNA polymerase proximal promoter sequence-specific DNA binding; IDA:EcoCyc.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
GO; GO:0051409; P:response to nitrosative stress; IDA:EcoCyc.
GO; GO:0006979; P:response to oxidative stress; IDA:EcoCyc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR005119; LysR_subst-bd.
InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00126; HTH_1; 1.
Pfam; PF03466; LysR_substrate; 1.
PRINTS; PR00039; HTHLYSR.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS50931; HTH_LYSR; 1.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; Direct protein sequencing;
Disulfide bond; DNA-binding; Glutathionylation; Oxidation;
Reference proteome; S-nitrosylation; Transcription;
Transcription regulation.
CHAIN 1 305 Hydrogen peroxide-inducible genes
activator.
/FTId=PRO_0000105728.
DOMAIN 1 58 HTH lysR-type. {ECO:0000255|PROSITE-
ProRule:PRU00253}.
DNA_BIND 18 37 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00253}.
MOD_RES 199 199 Cysteine sulfenic acid (-SOH); alternate.
{ECO:0000269|PubMed:12015987}.
MOD_RES 199 199 S-glutathionyl cysteine; alternate.
{ECO:0000269|PubMed:12015987}.
MOD_RES 199 199 S-nitrosocysteine; alternate.
{ECO:0000269|PubMed:12015987}.
DISULFID 180 259 {ECO:0000269|PubMed:12015987}.
DISULFID 199 208 Alternate. {ECO:0000269|PubMed:9497290}.
MUTAGEN 199 199 C->S,A: No activation following redox
signaling. {ECO:0000269|PubMed:9497290}.
MUTAGEN 208 208 C->S,A: No activation following redox
signaling. {ECO:0000269|PubMed:9497290}.
CONFLICT 154 154 A -> R (in Ref. 2; AAA24257).
{ECO:0000305}.
CONFLICT 249 249 R -> A (in Ref. 4; AAA24176).
{ECO:0000305}.
STRAND 91 97 {ECO:0000244|PDB:1I6A}.
TURN 99 101 {ECO:0000244|PDB:1I6A}.
HELIX 102 116 {ECO:0000244|PDB:1I6A}.
STRAND 120 126 {ECO:0000244|PDB:1I6A}.
HELIX 129 137 {ECO:0000244|PDB:1I6A}.
STRAND 142 147 {ECO:0000244|PDB:1I6A}.
HELIX 150 152 {ECO:0000244|PDB:1I6A}.
STRAND 155 170 {ECO:0000244|PDB:1I6A}.
HELIX 174 177 {ECO:0000244|PDB:1I6A}.
HELIX 183 186 {ECO:0000244|PDB:1I6A}.
STRAND 189 192 {ECO:0000244|PDB:1I6A}.
TURN 195 198 {ECO:0000244|PDB:1I6A}.
HELIX 201 203 {ECO:0000244|PDB:1I69}.
STRAND 213 216 {ECO:0000244|PDB:1I6A}.
TURN 218 221 {ECO:0000244|PDB:1I6A}.
HELIX 224 232 {ECO:0000244|PDB:1I6A}.
STRAND 237 241 {ECO:0000244|PDB:1I6A}.
HELIX 242 244 {ECO:0000244|PDB:1I6A}.
STRAND 247 251 {ECO:0000244|PDB:1I6A}.
STRAND 254 257 {ECO:0000244|PDB:1I6A}.
STRAND 259 262 {ECO:0000244|PDB:1I6A}.
STRAND 265 272 {ECO:0000244|PDB:1I6A}.
HELIX 279 293 {ECO:0000244|PDB:1I6A}.
TURN 294 297 {ECO:0000244|PDB:1I6A}.
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


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