Difference between revisions of "BdbD"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[bdbC]]'', ''[[cadA]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[bdbC]]'', ''[[cadA]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU33480 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU33480 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU33480 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU33480 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU33480 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU33480 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:bdbD_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:bdbD_context.gif]]

Revision as of 11:16, 14 May 2013

  • 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
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)