SigW
- Description: RNA polymerase ECF-type sigma factor SigW, activated by alkaline shock and by polymyxin B, vancomycin, cephalosporin C, D-cycloserine, and triton X-100
Gene name | sigW |
Synonyms | ybbL |
Essential | no |
Product | RNA polymerase ECF-type sigma factor SigW |
Function | resistance against SdpC that functions in detoxification and/or production of antimicrobial compounds |
Interactions involving this protein in SubtInteract: SigW | |
MW, pI | 21 kDa, 8.614 |
Gene length, protein length | 561 bp, 187 aa |
Immediate neighbours | trnSL-Gln2, ybbM |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
transcription, sigma factors and their control, cell envelope stress proteins (controlled by SigM, W, X, Y)
This gene is a member of the following regulons
The SigW regulon
The gene
Basic information
- Locus tag: BSU01730
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: ECF subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: RsiW acts as antagonist of SigW (anti-SigW)
Database entries
- Structure:
- UniProt: Q45585
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
John Helmann, Cornell University, USA Homepage
Thomas Wiegert, University of Bayreuth, Germany Homepage
Your additional remarks
References
Additional publications: PubMed
The SigW regulon
Other original publications
Jessica C Zweers, Thomas Wiegert, Jan Maarten van Dijl
Stress-responsive systems set specific limits to the overproduction of membrane proteins in Bacillus subtilis.
Appl Environ Microbiol: 2009, 75(23);7356-64
[PubMed:19820159]
[WorldCat.org]
[DOI]
(I p)
John D Helmann
Deciphering a complex genetic regulatory network: the Bacillus subtilis sigmaW protein and intrinsic resistance to antimicrobial compounds.
Sci Prog: 2006, 89(Pt 3-4);243-66
[PubMed:17338440]
[WorldCat.org]
[DOI]
(P p)
Craig D Ellermeier, Richard Losick
Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis.
Genes Dev: 2006, 20(14);1911-22
[PubMed:16816000]
[WorldCat.org]
[DOI]
(P p)
Mika Yoshimura, Kei Asai, Yoshito Sadaie, Hirofumi Yoshikawa
Interaction of Bacillus subtilis extracytoplasmic function (ECF) sigma factors with the N-terminal regions of their potential anti-sigma factors.
Microbiology (Reading): 2004, 150(Pt 3);591-599
[PubMed:14993308]
[WorldCat.org]
[DOI]
(P p)
Leif Steil, Tamara Hoffmann, Ina Budde, Uwe Völker, Erhard Bremer
Genome-wide transcriptional profiling analysis of adaptation of Bacillus subtilis to high salinity.
J Bacteriol: 2003, 185(21);6358-70
[PubMed:14563871]
[WorldCat.org]
[DOI]
(P p)
Min Cao, Tao Wang, Rick Ye, John D Helmann
Antibiotics that inhibit cell wall biosynthesis induce expression of the Bacillus subtilis sigma(W) and sigma(M) regulons.
Mol Microbiol: 2002, 45(5);1267-76
[PubMed:12207695]
[WorldCat.org]
[DOI]
(P p)
Qiang Qian, Chien Y Lee, John D Helmann, Mark A Strauch
AbrB is a regulator of the sigma(W) regulon in Bacillus subtilis.
FEMS Microbiol Lett: 2002, 211(2);219-23
[PubMed:12076816]
[WorldCat.org]
[DOI]
(P p)
T Wiegert, G Homuth, S Versteeg, W Schumann
Alkaline shock induces the Bacillus subtilis sigma(W) regulon.
Mol Microbiol: 2001, 41(1);59-71
[PubMed:11454200]
[WorldCat.org]
[DOI]
(P p)
J Qiu, J D Helmann
The -10 region is a key promoter specificity determinant for the Bacillus subtilis extracytoplasmic-function sigma factors sigma(X) and sigma(W).
J Bacteriol: 2001, 183(6);1921-7
[PubMed:11222589]
[WorldCat.org]
[DOI]
(P p)