Difference between revisions of "SdpB"
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<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div> | ||
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+ | |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sdpB_3464762_3465733_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:sdpB_expression.png|500px]] | ||
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Revision as of 09:17, 23 April 2012
- Description: membrane protein
Gene name | sdpB |
Synonyms | yvaX |
Essential | no |
Product | unknown |
Function | unknown |
MW, pI | 37 kDa, 9.521 |
Gene length, protein length | 969 bp, 323 aa |
Immediate neighbours | sdpA, sdpC |
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
toxins, antitoxins and immunity against toxins, membrane proteins
This gene is a member of the following regulons
AbrB regulon, Rok regulon, Spo0A regulon
The gene
Basic information
- Locus tag: BSU33760
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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane PubMed
Database entries
- Structure:
- UniProt: O34616
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- 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
Reviews
Original Publications
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[WorldCat.org]
[DOI]
(I p)
Mark A Strauch, Benjamin G Bobay, John Cavanagh, Fude Yao, Angelo Wilson, Yoann Le Breton
Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.
J Bacteriol: 2007, 189(21);7720-32
[PubMed:17720793]
[WorldCat.org]
[DOI]
(P 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)
Masaya Fujita, José Eduardo González-Pastor, Richard Losick
High- and low-threshold genes in the Spo0A regulon of Bacillus subtilis.
J Bacteriol: 2005, 187(4);1357-68
[PubMed:15687200]
[WorldCat.org]
[DOI]
(P p)
Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647]
[WorldCat.org]
[DOI]
(P p)
José E González-Pastor, Errett C Hobbs, Richard Losick
Cannibalism by sporulating bacteria.
Science: 2003, 301(5632);510-3
[PubMed:12817086]
[WorldCat.org]
[DOI]
(I p)