Difference between revisions of "OhrB"
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* '''Domains:''' | * '''Domains:''' | ||
| − | * '''Modification:'''Cys55-Cys119 form catalytic disulfide bond | + | * '''Modification:''' Cys55-Cys119 form catalytic disulfide bond {{PubMed|18084074}} |
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
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=== Additional information=== | === Additional information=== | ||
| − | :* subject to Clp-dependent proteolysis upon glucose starvation | + | :* subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}} |
| + | |||
=Expression and regulation= | =Expression and regulation= | ||
| Line 108: | Line 109: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
| − | ** subject to Clp-dependent proteolysis upon glucose starvation | + | ** subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}} |
=Biological materials = | =Biological materials = | ||
Revision as of 15:33, 14 March 2012
- Description: general stress protein
| Gene name | ohrB |
| Synonyms | yzzE, ykzA |
| Essential | no |
| Product | unknown |
| Function | organic peroxide resistance |
| MW, pI | 14 kDa, 4.735 |
| Gene length, protein length | 408 bp, 136 aa |
| Immediate neighbours | ohrR, guaD |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
general stress proteins (controlled by SigB), resistance against oxidative and electrophile stress
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU13160
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: osmC/ohr family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: Cys55-Cys119 form catalytic disulfide bond PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 2BJO
- UniProt: P80242
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Operon: ohrB PubMed
- Regulatory mechanism:
- Additional information:
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
David R Cooper, Yogesh Surendranath, Yancho Devedjiev, Jakub Bielnicki, Zygmunt S Derewenda
Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state.
Acta Crystallogr D Biol Crystallogr: 2007, 63(Pt 12);1269-73
[PubMed:18084074]
[WorldCat.org]
[DOI]
(P p)
Dirk Höper, Uwe Völker, Michael Hecker
Comprehensive characterization of the contribution of individual SigB-dependent general stress genes to stress resistance of Bacillus subtilis.
J Bacteriol: 2005, 187(8);2810-26
[PubMed:15805528]
[WorldCat.org]
[DOI]
(P p)
M Fuangthong, S Atichartpongkul, S Mongkolsuk, J D Helmann
OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis.
J Bacteriol: 2001, 183(14);4134-41
[PubMed:11418552]
[WorldCat.org]
[DOI]
(P p)
U Völker, K K Andersen, H Antelmann, K M Devine, M Hecker
One of two osmC homologs in Bacillus subtilis is part of the sigmaB-dependent general stress regulon.
J Bacteriol: 1998, 180(16);4212-8
[PubMed:9696771]
[WorldCat.org]
[DOI]
(P p)
