Difference between revisions of "SigB"
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− | <pubmed> 8655572 | + | <pubmed> 22210769, 8655572, 3123466, 10369900,3112122, 8468294,8458834, 13129942, 6784117, 12867438, 3100810, 8253681, 12486038, 8764398,3027048, 15342585,17575448, 17586624,,3016731,11902719,14651641,10503549,15205443,6405278, 10383961, 15805528 6790515 116131, 39767581 19948797 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 13:30, 3 January 2012
- Description: RNA polymerase sigma factor SigB
Gene name | sigB |
Synonyms | rpoF |
Essential | no |
Product | RNA polymerase sigma factor SigB |
Function | general stress response |
Interactions involving this protein in SubtInteract: SigB | |
Metabolic function and regulation of this protein in SubtiPathways: Stress, Murein recycling | |
MW, pI | 29 kDa, 5.418 |
Gene length, protein length | 792 bp, 264 aa |
Immediate neighbours | rsbW, rsbX |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
transcription, sigma factors and their control, general stress proteins (controlled by SigB)
This gene is a member of the following regulons
The SigB regulon
The gene
Basic information
- Locus tag: BSU04730
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: SigB subfamily (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: P06574
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant: QB5344 (cat), available in the Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Bill Haldenwang, San Antonio, USA
- Chet Price, Davis, USA homepage
Your additional remarks
References
Reviews
Jon Marles-Wright, Richard J Lewis
The stressosome: molecular architecture of a signalling hub.
Biochem Soc Trans: 2010, 38(4);928-33
[PubMed:20658979]
[WorldCat.org]
[DOI]
(I p)
Peter Zuber
Management of oxidative stress in Bacillus.
Annu Rev Microbiol: 2009, 63;575-97
[PubMed:19575568]
[WorldCat.org]
[DOI]
(I p)
Michael Hecker, Jan Pané-Farré, Uwe Völker
SigB-dependent general stress response in Bacillus subtilis and related gram-positive bacteria.
Annu Rev Microbiol: 2007, 61;215-36
[PubMed:18035607]
[WorldCat.org]
[DOI]
(P p)
M Hecker, U Völker
General stress response of Bacillus subtilis and other bacteria.
Adv Microb Physiol: 2001, 44;35-91
[PubMed:11407115]
[WorldCat.org]
[DOI]
(P p)
M Hecker, U Völker
Non-specific, general and multiple stress resistance of growth-restricted Bacillus subtilis cells by the expression of the sigmaB regulon.
Mol Microbiol: 1998, 29(5);1129-36
[PubMed:9767581]
[WorldCat.org]
[DOI]
(P p)
Control of SigB activity by protein-protein interactions
Identification of the SigB regulon
Other publications
Locke JC, Young JW, Fontes M, Hernández Jiménez MJ, Elowitz MB Stochastic pulse regulation in bacterial stress response. Science. 2011 334:366-369. PubMed:21979936