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PSEAE:Q9HTL4

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Species (Taxon ID) Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG12228). (208964)
Gene Name(s) oxyR (ECO:0000313 with EMBL:AAG08729.1)
Protein Name(s) OxyR (ECO:0000313 with EMBL:AAG08729.1)
External Links
UniProt Q9HTL4
EMBL AE004091
PIR F82979
RefSeq NP_254031.1
ProteinModelPortal Q9HTL4
SMR Q9HTL4
STRING 208964.PA5344
DNASU 878254
EnsemblBacteria AAG08729
GeneID 878254
KEGG pae:PA5344
PATRIC 19845547
PseudoCAP PA5344
HOGENOM HOG000233514
InParanoid Q9HTL4
KO K04761
OMA CPEFARF
OrthoDB EOG6N6848
PhylomeDB Q9HTL4
Proteomes UP000002438
GO GO:0001071
GO:0003700
GO:0044212
GO:1900377
GO:2000147
GO:0046889
GO:1901671
GO:1901031
GO:0006351
Gene3D 1.10.10.10
InterPro IPR005119
IPR000847
IPR011991
Pfam PF00126
PF03466
PRINTS PR00039
PROSITE PS50931

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0042542

response to hydrogen peroxide

PMID:19456869[1]

ECO:0000315

P

Fig. 1A (Lane 2), Fig. 1B (Lane 2)

complete

GO:0001071

nucleic acid binding transcription factor activity

PMID:22275523[2]

ECO:0000314

F

EMSA results in figure 2 prove OxyR binds to the promoter regions of several P. aerugenosa genes. Additionally, figure 3 shows that expression of dps, pvdS and trxB2 genes increased in the presence of OxyR activated by H2O2.

complete
CACAO 7589

enables

GO:0043565

sequence-specific DNA binding

PMID:19933365[3]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_008463.1

F

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:19933365[3]

ECO:0005620

chromatin immunoprecipitation-PCR evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

PMID:19933365[3]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:22275523[2]

ECO:0006007

chromatin immunoprecipitation-chip evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:19933365[3]

ECO:0005631

DNAse footprinting evidence used in manual assertion

RefSeq:NC_008463.1

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:19933365[3]

ECO:0005620

chromatin immunoprecipitation-PCR evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:22275523[2]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:19933365[3]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0032993

protein-DNA complex

PMID:10913087[4]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

PMID:22275523[2]

ECO:0001808

reverse transcription polymerase chain reaction evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0001216

DNA-binding transcription activator activity

PMID:10913087[4]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:22275523[2]

ECO:0006007

chromatin immunoprecipitation-chip evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:22275523[2]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000976

transcription regulatory region sequence-specific DNA binding

PMID:10913087[4]

ECO:0001807

electrophoretic mobility shift assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:2000147

positive regulation of cell motility

PMID:19926657[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1901671

positive regulation of superoxide dismutase activity

PMID:19926657[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1901031

regulation of response to reactive oxygen species

PMID:19933365[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1900377

negative regulation of secondary metabolite biosynthetic process

PMID:19926657[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046889

positive regulation of lipid biosynthetic process

PMID:19926657[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0044212

transcription regulatory region DNA binding

PMID:19933365[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0001216

P

Seeded From UniProt

complete

enables

GO:0003700

DNA-binding transcription factor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000847

F

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000847

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Panmanee, W & Hassett, DJ (2009) Differential roles of OxyR-controlled antioxidant enzymes alkyl hydroperoxide reductase (AhpCF) and catalase (KatB) in the protection of Pseudomonas aeruginosa against hydrogen peroxide in biofilm vs. planktonic culture. FEMS Microbiol. Lett. 295 238-44 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 Wei, Q et al. (2012) Global regulation of gene expression by OxyR in an important human opportunistic pathogen. Nucleic Acids Res. 40 4320-33 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 Heo, YJ et al. (2010) The major catalase gene (katA) of Pseudomonas aeruginosa PA14 is under both positive and negative control of the global transactivator OxyR in response to hydrogen peroxide. J. Bacteriol. 192 381-90 PubMed GONUTS page
  4. 4.0 4.1 4.2 Ochsner, UA et al. (2000) Role of the Pseudomonas aeruginosa oxyR-recG operon in oxidative stress defense and DNA repair: OxyR-dependent regulation of katB-ankB, ahpB, and ahpC-ahpF. J. Bacteriol. 182 4533-44 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 Vinckx, T et al. (2010) The Pseudomonas aeruginosa oxidative stress regulator OxyR influences production of pyocyanin and rhamnolipids: protective role of pyocyanin. Microbiology (Reading, Engl.) 156 678-86 PubMed GONUTS page