Difference between revisions of "OhrR"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13150&redirect=T BSU13150] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ykmA.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ykmA.html] | ||
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13150&redirect=T BSU13150] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1Z91 1Z91] (reduced form), [http://www.rcsb.org/pdb/explore.do?structureId=1Z9C 1Z9C] (complex with ''[[ohrA]]'' promoter) | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1Z91 1Z91] (reduced form), [http://www.rcsb.org/pdb/explore.do?structureId=1Z9C 1Z9C] (complex with ''[[ohrA]]'' promoter) | ||
| Line 120: | Line 122: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 133 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = | ||
| Line 144: | Line 147: | ||
=References= | =References= | ||
==Reviews== | ==Reviews== | ||
| − | <pubmed>22797754 20626317 19575568 20094649 </pubmed> | + | <pubmed>22797754 20626317 19575568 20094649 25852656</pubmed> |
==Original Publications== | ==Original Publications== | ||
<pubmed>21749987,16209951,18487332,17660290,17502599,12486061,11418552,18586944,11983871,18363800,19129220 9696771 21749987 22797754 24313874 </pubmed> | <pubmed>21749987,16209951,18487332,17660290,17502599,12486061,11418552,18586944,11983871,18363800,19129220 9696771 21749987 22797754 24313874 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Latest revision as of 11:02, 10 April 2015
- 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
| |
Contents
Categories containing this gene/protein
transcription factors and their control, resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The OhrR regulon:
The gene
Basic information
- Locus tag: BSU13150
Phenotypes of a mutant
Database entries
- BsubCyc: BSU13150
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: MarR family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU13150
- UniProt: O34777
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: ohrR PubMed
- 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
Your additional remarks
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)
Original Publications
