Difference between revisions of "BdbA"
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bdbA_2266936_2267349_-1 bdbA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=bdbA_2266936_2267349_-1 bdbA] {{PubMed|22383849}} | ||
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* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 20:23, 18 June 2013
- Description: thiol-disulfide oxidoreductase
Gene name | bdbA |
Synonyms | yolI |
Essential | no |
Product | thiol-disulfide oxidoreductase |
Function | oxidative folding of proteins |
Gene expression levels in SubtiExpress: bdbA | |
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion | |
MW, pI | 16 kDa, 8.337 |
Gene length, protein length | 411 bp, 137 aa |
Immediate neighbours | sunS, sunT |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
chaperones/ protein folding, SP-beta prophage
This gene is a member of the following regulons
Abh regulon, AbrB regulon Rok regulon, YvrHb regulon
The gene
Basic information
- Locus tag: BSU21460
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: thioredoxin family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P68569
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947]
[WorldCat.org]
[DOI]
(I p)
Onuma Chumsakul, Hiroki Takahashi, Taku Oshima, Takahiro Hishimoto, Shigehiko Kanaya, Naotake Ogasawara, Shu Ishikawa
Genome-wide binding profiles of the Bacillus subtilis transition state regulator AbrB and its homolog Abh reveals their interactive role in transcriptional regulation.
Nucleic Acids Res: 2011, 39(2);414-28
[PubMed:20817675]
[WorldCat.org]
[DOI]
(I p)
Mark Albano, Wiep Klaas Smits, Linh T Y Ho, Barbara Kraigher, Ines Mandic-Mulec, Oscar P Kuipers, David Dubnau
The Rok protein of Bacillus subtilis represses genes for cell surface and extracellular functions.
J Bacteriol: 2005, 187(6);2010-9
[PubMed:15743949]
[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)