Difference between revisions of "BdbC"

From SubtiWiki
Jump to: navigation, search
Line 1: Line 1:
* '''Description:''' thiol-disulfide oxidoreductase, required for the formation of thiol disulfide bonds in [[ComGC]] <br/><br/>
+
* '''Description:''' thiol-disulfide oxidoreductase, required for the formation of thiol disulfide bonds in several proteins <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
Line 76: Line 76:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:''' formation of thiol disulfide bonds in [[ComGC]] [http://www.ncbi.nlm.nih.gov/sites/entrez/11744713 PubMed]
+
* '''Catalyzed reaction/ biological activity:'''  
 +
** formation of thiol disulfide bonds in [[ComEC]] and [[ComGC]] (together with [[BdbD]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/11744713 PubMed]
 +
** oxidative folding of [[SunA]] (together with [[BdbB]])
  
 
* '''Protein family:''' BdbC subfamily (according to Swiss-Prot)
 
* '''Protein family:''' BdbC subfamily (according to Swiss-Prot)

Revision as of 14:23, 6 May 2012

  • Description: thiol-disulfide oxidoreductase, required for the formation of thiol disulfide bonds in several proteins

Gene name bdbC
Synonyms yvgU
Essential no
Product thiol-disulfide oxidoreductase
Function genetic transformation
Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 15 kDa, 9.054
Gene length, protein length 414 bp, 138 aa
Immediate neighbours yvgT, bdbD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
BdbC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
BdbC expression.png
























Categories containing this gene/protein

genetic competence, chaperones/ protein folding, sporulation proteins, membrane proteins

This gene is a member of the following regulons

ComK regulon, SigE regulon

The gene

Basic information

  • Locus tag: BSU33470

Phenotypes of a mutant

loss of transformability PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: BdbC subfamily (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

  • Regulation:
    • expressed early during sporulation in the mother cell (SigE) PubMed
  • Regulatory mechanism:
  • 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

Elise Darmon, Ronald Dorenbos, Jochen Meens, Roland Freudl, Haike Antelmann, Michael Hecker, Oscar P Kuipers, Sierd Bron, Wim J Quax, Jean-Yves F Dubois, Jan Maarten van Dijl
A disulfide bond-containing alkaline phosphatase triggers a BdbC-dependent secretion stress response in Bacillus subtilis.
Appl Environ Microbiol: 2006, 72(11);6876-85
[PubMed:17088376] [WorldCat.org] [DOI] (P p)

Inês Chen, Roberta Provvedi, David Dubnau
A macromolecular complex formed by a pilin-like protein in competent Bacillus subtilis.
J Biol Chem: 2006, 281(31);21720-21727
[PubMed:16751195] [WorldCat.org] [DOI] (P p)

Irena Draskovic, David Dubnau
Biogenesis of a putative channel protein, ComEC, required for DNA uptake: membrane topology, oligomerization and formation of disulphide bonds.
Mol Microbiol: 2005, 55(3);881-96
[PubMed:15661011] [WorldCat.org] [DOI] (P p)

Ritsuko Kuwana, Yasuhiro Kasahara, Machiko Fujibayashi, Hiromu Takamatsu, Naotake Ogasawara, Kazuhito Watabe
Proteomics characterization of novel spore proteins of Bacillus subtilis.
Microbiology (Reading): 2002, 148(Pt 12);3971-3982
[PubMed:12480901] [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)

Lýdur S Erlendsson, Lars Hederstedt
Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells.
J Bacteriol: 2002, 184(5);1423-9
[PubMed:11844773] [WorldCat.org] [DOI] (P p)

Rob Meima, Caroline Eschevins, Sabine Fillinger, Albert Bolhuis, Leendert W Hamoen, Ronald Dorenbos, Wim J Quax, Jan Maarten van Dijl, Roberta Provvedi, Ines Chen, David Dubnau, Sierd Bron
The bdbDC operon of Bacillus subtilis encodes thiol-disulfide oxidoreductases required for competence development.
J Biol Chem: 2002, 277(9);6994-7001
[PubMed:11744713] [WorldCat.org] [DOI] (P p)