Difference between revisions of "BdbC"
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|style="background:#ABCDEF;" align="center"| '''Product''' || thiol-disulfide oxidoreductase | |style="background:#ABCDEF;" align="center"| '''Product''' || thiol-disulfide oxidoreductase | ||
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− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |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]], [[ProA]], [[PyrAA]], [[PyrAB]], [[PyrH]], [[PyrE]], [[PyrF]], [[DegS]], [[YbxA]] {{PubMed|22540663}} | ||
=== Database entries === | === Database entries === | ||
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=== Additional information=== | === Additional information=== | ||
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=References= | =References= | ||
− | <pubmed>11744713,15661011,11872755,17088376,16751195,11844773,12480901 , </pubmed> | + | <pubmed>11744713,15661011,11872755,17088376,16751195,11844773,12480901 , 22540663 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 14:40, 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 | oxidative folding of proteins |
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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
genetic competence, chaperones/ protein folding, sporulation proteins, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU33470
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
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:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: O32217
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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)
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)