BdbD

• 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
Gene expression levels in SubtiExpress: bdbD
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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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
• sensitive to osmotic shock PubMed
• several proteins are absent from the membrane proteome of a bdbC-bdbD mutant: PubMed
  • the membrane proteins BglP, TcyP, SipU, LytA, and YxaI PubMed
  • the cytoplasmic or membrane-associated proteins GlkX, ProA, PyrAA, PyrAB, PyrH, PyrE, PyrF, DegS, YbxA PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • formation of thiol disulfide bonds in ComEC and ComGC (together with BdbC) 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

• Expression browser: bdbD 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

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)