BdbD

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

Gene name	bdbD
Synonyms	yvgV
Essential	no
Product	thiol-disulfide oxidoreductase
Function	genetic transformation
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 This image was kindly provided by SubtiList

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

loss of transformability PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: formation of thiol disulfide bonds in ComGC PubMed

• Protein family: DsbA subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s): Ca (2+) PubMed

• Effectors of protein activity:

• Interactions:

• Localization: membrane, faced to the outer side of the membrane PubMed

Database entries

• Structure: 3EU3 (reduced form), 3EU4 (oxidized form) PubMed

• UniProt: O32218

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: bdbD-bdbC PubMed

• Sigma factor: SigE PubMed

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

• Regulatory mechanism:
  • ComK: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)