Difference between revisions of "SigB"
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** ''[[rsbV]]-[[rsbW]]-[[sigB]]-[[rsbX]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/2170324 PubMed] | ** ''[[rsbV]]-[[rsbW]]-[[sigB]]-[[rsbX]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/2170324 PubMed] | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sigB_522862_523650_1 sigB] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' | ||
** ''[[rsbR]]'': [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8002610 PubMed] | ** ''[[rsbR]]'': [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8002610 PubMed] | ||
** ''[[rsbV]]:'' [[SigB]] [http://www.ncbi.nlm.nih.gov/pubmed/11544224 PubMed] | ** ''[[rsbV]]:'' [[SigB]] [http://www.ncbi.nlm.nih.gov/pubmed/11544224 PubMed] |
Revision as of 14:50, 12 April 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
Control of SigB activity by protein-protein interactions
Oleg A Igoshin, Margaret S Brody, Chester W Price, Michael A Savageau
Distinctive topologies of partner-switching signaling networks correlate with their physiological roles.
J Mol Biol: 2007, 369(5);1333-52
[PubMed:17498739]
[WorldCat.org]
[DOI]
(P p)
Tae-Jong Kim, Tatiana A Gaidenko, Chester W Price
In vivo phosphorylation of partner switching regulators correlates with stress transmission in the environmental signaling pathway of Bacillus subtilis.
J Bacteriol: 2004, 186(18);6124-32
[PubMed:15342582]
[WorldCat.org]
[DOI]
(P p)
Tae-Jong Kim, Tatiana A Gaidenko, Chester W Price
A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis.
J Mol Biol: 2004, 341(1);135-50
[PubMed:15312768]
[WorldCat.org]
[DOI]
(P p)
Olivier Delumeau, Richard J Lewis, Michael D Yudkin
Protein-protein interactions that regulate the energy stress activation of sigma(B) in Bacillus subtilis.
J Bacteriol: 2002, 184(20);5583-9
[PubMed:12270815]
[WorldCat.org]
[DOI]
(P p)
M S Brody, K Vijay, C W Price
Catalytic function of an alpha/beta hydrolase is required for energy stress activation of the sigma(B) transcription factor in Bacillus subtilis.
J Bacteriol: 2001, 183(21);6422-8
[PubMed:11591687]
[WorldCat.org]
[DOI]
(P p)
C Eymann, M Hecker
Induction of sigma(B)-dependent general stress genes by amino acid starvation in a spo0H mutant of Bacillus subtilis.
FEMS Microbiol Lett: 2001, 199(2);221-7
[PubMed:11377871]
[WorldCat.org]
[DOI]
(P p)
A Dufour, U Voelker, A Voelker, W G Haldenwang
Relative levels and fractionation properties of Bacillus subtilis σ(B) and its regulators during balanced growth and stress.
J Bacteriol: 1996, 178(13);3701-9 sigma
[PubMed:8682769]
[WorldCat.org]
[DOI]
(P p)
U Voelker, A Voelker, B Maul, M Hecker, A Dufour, W G Haldenwang
Separate mechanisms activate sigma B of Bacillus subtilis in response to environmental and metabolic stresses.
J Bacteriol: 1995, 177(13);3771-80
[PubMed:7601843]
[WorldCat.org]
[DOI]
(P p)
A A Wise, C W Price
Four additional genes in the sigB operon of Bacillus subtilis that control activity of the general stress factor sigma B in response to environmental signals.
J Bacteriol: 1995, 177(1);123-33
[PubMed:8002610]
[WorldCat.org]
[DOI]
(P p)
A K Benson, W G Haldenwang
Bacillus subtilis sigma B is regulated by a binding protein (RsbW) that blocks its association with core RNA polymerase.
Proc Natl Acad Sci U S A: 1993, 90(6);2330-4
[PubMed:8460143]
[WorldCat.org]
[DOI]
(P p)
Identification of the SigB regulon
Other publications
Additional publications: PubMed
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