Difference between revisions of "BdbB"

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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bdbB_2265225_2265671_-1 bdbB] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bdbB_2265225_2265671_-1 bdbB] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
'''Additional publications:''' {{PubMed|20817675}}
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<pubmed>11872755 15743949,20817675 </pubmed>
<pubmed>11872755 15743949, </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 20:19, 18 June 2013

  • Description: thiol-disulfide oxidoreductase

Gene name bdbB
Synonyms yolK
Essential no
Product thiol-disulfide oxidoreductase
Function oxidative folding of proteins
Gene expression levels in SubtiExpress: bdbB
Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 16 kDa, 9.415
Gene length, protein length 444 bp, 148 aa
Immediate neighbours bhlB, sunS
Sequences Protein DNA DNA_with_flanks
Genetic context
BdbB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
BdbB expression.png















Categories containing this gene/protein

chaperones/ protein folding, SP-beta prophage, membrane proteins

This gene is a member of the following regulons

Abh regulon, AbrB regulon, Rok regulon, YvrHb regulon

The gene

Basic information

  • Locus tag: BSU21440

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • oxidative folding of SunA (together with BdbC)
  • Protein family: NAD-dependent glycerol-3-phosphate dehydrogenase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675] [WorldCat.org] [DOI] (I p)

Mark Albano, Wiep Klaas Smits, Linh T Y Ho, Barbara Kraigher, Ines Mandic-Mulec, Oscar P Kuipers, David Dubnau
The Rok protein of Bacillus subtilis represses genes for cell surface and extracellular functions.
J Bacteriol: 2005, 187(6);2010-9
[PubMed:15743949] [WorldCat.org] [DOI] (P p)

Ronald Dorenbos, Torsten Stein, Jorrit Kabel, Claude Bruand, Albert Bolhuis, Sierd Bron, Wim J Quax, Jan Maarten Van Dijl
Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168.
J Biol Chem: 2002, 277(19);16682-8
[PubMed:11872755] [WorldCat.org] [DOI] (P p)