Difference between revisions of "BdbD"

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* '''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"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || thiol-disulfide oxidoreductase
 
|style="background:#ABCDEF;" align="center"| '''Product''' || thiol-disulfide oxidoreductase
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || genetic transformation
+
|style="background:#ABCDEF;" align="center"|'''Function''' || oxidative folding of proteins
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]'''
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 
+
* loss of transformability [http://www.ncbi.nlm.nih.gov/sites/entrez/11744713 PubMed]
loss of transformability [http://www.ncbi.nlm.nih.gov/sites/entrez/11744713 PubMed]
+
* sensitive to osmotic shock {{PubMed|22540663}}
 +
* several proteins are absent from the membrane proteome of a ''[[bdbC]]-[[bdbD]]'' mutant: {{PubMed|22540663}}
 +
** the membrane proteins [[BglP]], [[TcyP]], [[SipU]], [[LytA]], and [[YxaI]] {{PubMed|22540663}}
 +
** the cytoplasmic or membrane-associated proteins [[GlkX]], [[PyrAA]], [[PyrAB]], [[PyrH]], [[PyrE]], [[PyrF]], [[DegS]], [[YbxA]] {{PubMed|22540663}}
  
 
=== Database entries ===
 
=== Database entries ===
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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=== 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 [[BdbC]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/11744713 PubMed]
  
 
* '''Protein family:''' DsbA subfamily (according to Swiss-Prot)
 
* '''Protein family:''' DsbA subfamily (according to Swiss-Prot)
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=References=
 
=References=
  
<pubmed>19535335, 11744713,15661011,11872755,16751195,11844773, 12480901</pubmed>
+
<pubmed>19535335, 11744713,15661011,11872755,16751195,11844773, 12480901 22540663 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:35, 6 May 2012

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

Gene name bdbD
Synonyms yvgV
Essential no
Product thiol-disulfide oxidoreductase
Function oxidative folding of proteins
Metabolic function and regulation of this protein in SubtiPathways:
Protein secretion
MW, pI 24 kDa, 5.089
Gene length, protein length 666 bp, 222 aa
Immediate neighbours bdbC, cadA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
BdbD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
BdbD 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: BSU33480

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: DsbA subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Effectors of protein activity:

Database entries

  • 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

Vivianne J Goosens, Ruben A T Mars, Michiel Akeroyd, Andre Vente, Annette Dreisbach, Emma L Denham, Thijs R H M Kouwen, Tjeerd van Rij, Maurien Olsthoorn, Jan Maarten van Dijl
Is proteomics a reliable tool to probe the oxidative folding of bacterial membrane proteins?
Antioxid Redox Signal: 2013, 18(10);1159-64
[PubMed:22540663] [WorldCat.org] [DOI] (I p)

Allister Crow, Allison Lewin, Oliver Hecht, Mirja Carlsson Möller, Geoffrey R Moore, Lars Hederstedt, Nick E Le Brun
Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:disulfide oxidoreductase containing a novel metal site.
J Biol Chem: 2009, 284(35);23719-33
[PubMed:19535335] [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)