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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)DescriptionActionsGraphical viewLength
DNA bindingi18 – 37H-T-H motifPROSITE-ProRule annotationAdd BLAST20

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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi199C → S or A: No activation following redox signaling. 1 Publication1
Mutagenesisi208C → S or A: No activation following redox signaling. 1 Publication1

Chemistry databases

DrugBankiDB03793. Benzoic Acid.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001057281 – 305Hydrogen peroxide-inducible genes activatorAdd BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi180 ↔ 2591 Publication
Disulfide bondi199 ↔ 208Alternate1 Publication
Modified residuei199Cysteine sulfenic acid (-SOH); alternate1 Publication1
Modified residuei199S-glutathionyl cysteine; alternate1 Publication1
Modified residuei199S-nitrosocysteine; alternate1 Publication1

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 interactors.
DIPiDIP-10419N.
IntActiP0ACQ4. 2 interactors.
STRINGi511145.b3961.

Structurei

Secondary structure

1305
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi91 – 97Combined sources7
Turni99 – 101Combined sources3
Helixi102 – 116Combined sources15
Beta strandi120 – 126Combined sources7
Helixi129 – 137Combined sources9
Beta strandi142 – 147Combined sources6
Helixi150 – 152Combined sources3
Beta strandi155 – 170Combined sources16
Helixi174 – 177Combined sources4
Helixi183 – 186Combined sources4
Beta strandi189 – 192Combined sources4
Turni195 – 198Combined sources4
Helixi201 – 203Combined sources3
Beta strandi213 – 216Combined sources4
Turni218 – 221Combined sources4
Helixi224 – 232Combined sources9
Beta strandi237 – 241Combined sources5
Helixi242 – 244Combined sources3
Beta strandi247 – 251Combined sources5
Beta strandi254 – 257Combined sources4
Beta strandi259 – 262Combined sources4
Beta strandi265 – 272Combined sources8
Helixi279 – 293Combined sources15
Turni294 – 297Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0ACQ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 58HTH lysR-typePROSITE-ProRule annotationAdd BLAST58

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C5Q. Bacteria.
ENOG410XNR2. LUCA.
HOGENOMiHOG000233514.
InParanoidiP0ACQ4.
KOiK04761.
OMAiCPEFARF.
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)DescriptionActionsGraphical viewLength
Sequence conflicti154A → R in AAA24257 (PubMed:2551682).Curated1
Sequence conflicti249R → A in AAA24176 (PubMed:2167922).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I69X-ray2.70A/B87-305[»]
1I6AX-ray2.30A87-305[»]
ProteinModelPortaliP0ACQ4.
SMRiP0ACQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

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.
PhylomeDBiP0ACQ4.

Enzyme and pathway databases

BioCyciEcoCyc:PD00214.
ECOL316407:JW3933-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...

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: November 2, 2016
This is version 96 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.