Difference between revisions of "OhrB"

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* '''Domains:'''  
 
* '''Domains:'''  
  
* '''Modification:'''Cys55-Cys119 form catalytic disulfide bond  
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* '''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 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
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:* subject to Clp-dependent proteolysis upon glucose starvation {{PubMed|17981983}}
 +
 
 
=Expression and regulation=
 
=Expression and regulation=
  
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* '''Additional information:'''  
 
* '''Additional information:'''  
** subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
+
** 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
YkzA context.gif
This image was kindly provided by SubtiList



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

SigB regulon

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

  • KEGG entry: [3]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • 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)