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Protein

Hydrogen peroxide-inducible genes activator

Gene

oxyR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

Activated by oxidation of Cys-199 resulting in the alternative formation of cystine, sulfenic acid, S-nitroso- or glutathione-bound cysteine.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi18 – 3720H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • regulation of DNA-templated transcription, initiation Source: EcoCyc
  • response to nitrosative stress Source: EcoCyc
  • response to oxidative stress Source: EcoCyc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00214.
ECOL316407:JW3933-MONOMER.
RETL1328306-WGS:GSTH-4242-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydrogen peroxide-inducible genes activator
Alternative name(s):
Morphology and auto-aggregation control protein
Gene namesi
Name:oxyR
Synonyms:momR, mor
Ordered Locus Names:b3961, JW3933
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10681. oxyR.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991C → S or A: No activation following redox signaling. 1 Publication
Mutagenesisi208 – 2081C → S or A: No activation following redox signaling. 1 Publication

Chemistry

DrugBankiDB03793. Benzoic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305Hydrogen peroxide-inducible genes activatorPRO_0000105728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi180 ↔ 2591 Publication
Disulfide bondi199 ↔ 208Alternate1 Publication
Modified residuei199 – 1991Cysteine sulfenic acid (-SOH); alternate1 Publication
Modified residuei199 – 1991S-glutathionyl cysteine; alternate1 Publication
Modified residuei199 – 1991S-nitrosocysteine; alternate1 Publication

Post-translational modificationi

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.1 Publication
S-nitrosylation in response to nitrosative signaling triggers a conformational change and the onset of transcriptional activity with a specific DNA-binding affinity.1 Publication
Glutathionylation in response to redox signaling triggers the onset of transcriptional activity with a specific DNA-binding affinity.1 Publication

Keywords - PTMi

Disulfide bond, Glutathionylation, Oxidation, S-nitrosylation

Proteomic databases

EPDiP0ACQ4.
PaxDbiP0ACQ4.
PRIDEiP0ACQ4.

Interactioni

Subunit structurei

Homodimer and homotetramer.

Protein-protein interaction databases

BioGridi4263457. 5 interactions.
DIPiDIP-10419N.
IntActiP0ACQ4. 2 interactions.
STRINGi511145.b3961.

Structurei

Secondary structure

1
305
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi91 – 977Combined sources
Turni99 – 1013Combined sources
Helixi102 – 11615Combined sources
Beta strandi120 – 1267Combined sources
Helixi129 – 1379Combined sources
Beta strandi142 – 1476Combined sources
Helixi150 – 1523Combined sources
Beta strandi155 – 17016Combined sources
Helixi174 – 1774Combined sources
Helixi183 – 1864Combined sources
Beta strandi189 – 1924Combined sources
Turni195 – 1984Combined sources
Helixi201 – 2033Combined sources
Beta strandi213 – 2164Combined sources
Turni218 – 2214Combined sources
Helixi224 – 2329Combined sources
Beta strandi237 – 2415Combined sources
Helixi242 – 2443Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi254 – 2574Combined sources
Beta strandi259 – 2624Combined sources
Beta strandi265 – 2728Combined sources
Helixi279 – 29315Combined sources
Turni294 – 2974Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I69X-ray2.70A/B87-305[»]
1I6AX-ray2.30A87-305[»]
ProteinModelPortaliP0ACQ4.
SMRiP0ACQ4. Positions 1-298.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACQ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858HTH lysR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH lysR-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105C5Q. Bacteria.
ENOG410XNR2. LUCA.
HOGENOMiHOG000233514.
InParanoidiP0ACQ4.
KOiK04761.
OMAiCPEFARF.
OrthoDBiEOG6N6848.
PhylomeDBiP0ACQ4.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005119. LysR_subst-bd.
IPR000847. Tscrpt_reg_HTH_LysR.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00126. HTH_1. 1 hit.
PF03466. LysR_substrate. 1 hit.
[Graphical view]
PRINTSiPR00039. HTHLYSR.
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50931. HTH_LYSR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ACQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIRDLEYLV ALAEHRHFRR AADSCHVSQP TLSGQIRKLE DELGVMLLER
60 70 80 90 100
TSRKVLFTQA GMLLVDQART VLREVKVLKE MASQQGETMS GPLHIGLIPT
110 120 130 140 150
VGPYLLPHII PMLHQTFPKL EMYLHEAQTH QLLAQLDSGK LDCVILALVK
160 170 180 190 200
ESEAFIEVPL FDEPMLLAIY EDHPWANREC VPMADLAGEK LLMLEDGHCL
210 220 230 240 250
RDQAMGFCFE AGADEDTHFR ATSLETLRNM VAAGSGITLL PALAVPPERK
260 270 280 290 300
RDGVVYLPCI KPEPRRTIGL VYRPGSPLRS RYEQLAEAIR ARMDGHFDKV

LKQAV
Length:305
Mass (Da):34,276
Last modified:November 22, 2005 - v1
Checksum:i714EF4169CED2EC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541A → R in AAA24257 (PubMed:2551682).Curated
Sequence conflicti249 – 2491R → A in AAA24176 (PubMed:2167922).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04553 Genomic DNA. Translation: AAA24257.1.
X52666 Genomic DNA. Translation: CAA36893.1.
X16531 Genomic DNA. Translation: CAA34534.1.
M34102 Genomic DNA. Translation: AAA24176.1.
U00006 Genomic DNA. Translation: AAC43067.1.
U00096 Genomic DNA. Translation: AAC76943.1.
AP009048 Genomic DNA. Translation: BAE77350.1.
PIRiD65203. RGECOX.
RefSeqiNP_418396.1. NC_000913.3.
WP_001025939.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76943; AAC76943; b3961.
BAE77350; BAE77350; BAE77350.
GeneIDi948462.
KEGGiecj:JW3933.
eco:b3961.
PATRICi32123443. VBIEscCol129921_4082.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04553 Genomic DNA. Translation: AAA24257.1.
X52666 Genomic DNA. Translation: CAA36893.1.
X16531 Genomic DNA. Translation: CAA34534.1.
M34102 Genomic DNA. Translation: AAA24176.1.
U00006 Genomic DNA. Translation: AAC43067.1.
U00096 Genomic DNA. Translation: AAC76943.1.
AP009048 Genomic DNA. Translation: BAE77350.1.
PIRiD65203. RGECOX.
RefSeqiNP_418396.1. NC_000913.3.
WP_001025939.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I69X-ray2.70A/B87-305[»]
1I6AX-ray2.30A87-305[»]
ProteinModelPortaliP0ACQ4.
SMRiP0ACQ4. Positions 1-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263457. 5 interactions.
DIPiDIP-10419N.
IntActiP0ACQ4. 2 interactions.
STRINGi511145.b3961.

Chemistry

DrugBankiDB03793. Benzoic Acid.

Proteomic databases

EPDiP0ACQ4.
PaxDbiP0ACQ4.
PRIDEiP0ACQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76943; AAC76943; b3961.
BAE77350; BAE77350; BAE77350.
GeneIDi948462.
KEGGiecj:JW3933.
eco:b3961.
PATRICi32123443. VBIEscCol129921_4082.

Organism-specific databases

EchoBASEiEB0675.
EcoGeneiEG10681. oxyR.

Phylogenomic databases

eggNOGiENOG4105C5Q. Bacteria.
ENOG410XNR2. LUCA.
HOGENOMiHOG000233514.
InParanoidiP0ACQ4.
KOiK04761.
OMAiCPEFARF.
OrthoDBiEOG6N6848.
PhylomeDBiP0ACQ4.

Enzyme and pathway databases

BioCyciEcoCyc:PD00214.
ECOL316407:JW3933-MONOMER.
RETL1328306-WGS:GSTH-4242-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ACQ4.
PROiP0ACQ4.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005119. LysR_subst-bd.
IPR000847. Tscrpt_reg_HTH_LysR.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00126. HTH_1. 1 hit.
PF03466. LysR_substrate. 1 hit.
[Graphical view]
PRINTSiPR00039. HTHLYSR.
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50931. HTH_LYSR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins."
    Christman M.F., Storz G., Ames B.N.
    Proc. Natl. Acad. Sci. U.S.A. 86:3484-3488(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The Escherichia coli regulatory protein OxyR discriminates between methylated and unmethylated states of the phage Mu mom promoter."
    Boelker M., Kahmann R.
    EMBO J. 8:2403-2410(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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."
    Tao K., Makino K., Yonei S., Nakata A., Shinagawa H.
    Mol. Gen. Genet. 218:371-376(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Identification and characterization of a gene that controls colony morphology and auto-aggregation in Escherichia coli K12."
    Warne S.R., Varley J.M., Boulnois G.J., Norton M.G.
    J. Gen. Microbiol. 136:455-462(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  5. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Purification and characterization of the Escherichia coli OxyR protein, the positive regulator for a hydrogen peroxide-inducible regulon."
    Tao K., Makino K., Yonei S., Nakata A., Shinagawa H.
    J. Biochem. 109:262-266(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10.
  9. "Activation of the OxyR transcription factor by reversible disulfide bond formation."
    Zheng M., Aslund F., Storz G.
    Science 279:1718-1721(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISULFIDE BONDS, MUTAGENESIS OF CYS-199 AND CYS-208.
  10. Cited for: S-NITROSYLATION AT CYS-199, GLUTATHIONYLATION AT CYS-199, OXIDATION AT CYS-199, DISULFIDE BOND 180-CYS--CYS-259.

Entry informationi

Entry nameiOXYR_ECOLI
AccessioniPrimary (citable) accession number: P0ACQ4
Secondary accession number(s): P11721, P22471, Q2M8Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: March 16, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Oxidized OxyR can be reduced and inactivated by glutaredoxin 1, the product of grxA, whose expression is regulated by OxyR itself.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.