OhrR

• Description: transcription repressor of the ohrA gene
  
  

Gene name	ohrR
Synonyms	ykmA
Essential	no
Product	transcription repressor (MarR family)
Function	regulation of ohrA expression in response to organic peroxides
Gene expression levels in SubtiExpress: ohrR
Interactions involving this protein in SubtInteract: OhrR
MW, pI	16 kDa, 6.364
Gene length, protein length	441 bp, 147 aa
Immediate neighbours	ohrA, ohrB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transcription factors and their control, resistance against oxidative and electrophile stress

The OhrR regulon:

• ohrA

The gene

Basic information

• Locus tag: BSU13150

Database entries

• BsubCyc: BSU13150

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: MarR family

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • senses organic peroxides and NaOCl, released from DNA upon oxidation of an active site cysteine
  • S-bacillithiolated by NaOCl and CHP stress on Cys-15, this results in release from the ohrA promoter PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • forms dimers
  • BrxA-OhrR, to de-bacillithiolate S-bacillithiolated OhrR PubMed
  • BrxB-OhrR, to de-bacillithiolate S-bacillithiolated OhrR PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU13150

• Structure: 1Z91 (reduced form), 1Z9C (complex with ohrA promoter)

• UniProt: O34777

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ohrR PubMed

• Expression browser: ohrR PubMed

• Sigma factor: SigA

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 133 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

John Helmann, Cornell University, USA Homepage

Richard Brennan, Houston, Texas, USA Homepage

References

Reviews

Vu Van Loi, Martina Rossius, Haike Antelmann
Redox regulation by reversible protein S-thiolation in bacteria.
Front Microbiol: 2015, 6;187
[PubMed:25852656] [WorldCat.org] [DOI] (P e)

James M Dubbs, Skorn Mongkolsuk
Peroxide-sensing transcriptional regulators in bacteria.
J Bacteriol: 2012, 194(20);5495-503
[PubMed:22797754] [WorldCat.org] [DOI] (I p)

Haike Antelmann, John D Helmann
Thiol-based redox switches and gene regulation.
Antioxid Redox Signal: 2011, 14(6);1049-63
[PubMed:20626317] [WorldCat.org] [DOI] (I p)

Victor Duarte, Jean-Marc Latour
PerR vs OhrR: selective peroxide sensing in Bacillus subtilis.
Mol Biosyst: 2010, 6(2);316-23
[PubMed:20094649] [WorldCat.org] [DOI] (I p)

Peter Zuber
Management of oxidative stress in Bacillus.
Annu Rev Microbiol: 2009, 63;575-97
[PubMed:19575568] [WorldCat.org] [DOI] (I p)