RsbW

• Description: Anti-SigB, protein serine kinase, phosphorylates RsbV
  
  

Gene name	rsbW
Synonyms
Essential	no
Product	anti-SigB, protein serine kinase
Function	control of SigB activity
Gene expression levels in SubtiExpress: rsbW
Interactions involving this protein in SubtInteract: RsbW
Metabolic function and regulation of this protein in SubtiPathways: rsbW
MW, pI	17 kDa, 4.285
Gene length, protein length	480 bp, 160 aa
Immediate neighbours	rsbV, sigB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein modification, sigma factors and their control, general stress proteins (controlled by SigB)

This gene is a member of the following regulons

CcpA regulon, SigB regulon

The gene

Basic information

• Locus tag: BSU04720

Database entries

• BsubCyc: BSU04720

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + a protein = ADP + a phosphoprotein (according to Swiss-Prot)

• Protein family: anti-sigma-factor family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • RsbV-RsbW PubMed
  • SigB-RsbW PubMed

• Localization:

Database entries

• BsubCyc: BSU04720

• Structure:

• UniProt: P17904

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • rsbR-rsbS-rsbT-rsbU-rsbV-rsbW-sigB-rsbX PubMed
  • rsbV-rsbW-sigB-rsbX PubMed

• Expression browser: rsbW PubMed

• Sigma factor:
  • rsbR: SigA PubMed
  • rsbV: SigB PubMed

• Regulation:
  • rsbV: induced by stress (SigB) PubMed

• Additional information:

Biological materials

• Mutant:

• 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

References

Daina L Ringus, Ahmed Gaballa, John D Helmann, Martin Wiedmann, Kathryn J Boor
Fluoro-phenyl-styrene-sulfonamide, a novel inhibitor of σB activity, prevents the activation of σB by environmental and energy stresses in Bacillus subtilis.
J Bacteriol: 2013, 195(11);2509-17
[PubMed:23524614] [WorldCat.org] [DOI] (I p)

Jonathan W Young, James C W Locke, Michael B Elowitz
Rate of environmental change determines stress response specificity.
Proc Natl Acad Sci U S A: 2013, 110(10);4140-5
[PubMed:23407164] [WorldCat.org] [DOI] (I p)

James C W Locke, Jonathan W Young, Michelle Fontes, María Jesús Hernández Jiménez, Michael B Elowitz
Stochastic pulse regulation in bacterial stress response.
Science: 2011, 334(6054);366-9
[PubMed:21979936] [WorldCat.org] [DOI] (I p)

Gudrun Holtmann, Matthias Brigulla, Leif Steil, Alexandra Schütz, Karsta Barnekow, Uwe Völker, Erhard Bremer
RsbV-independent induction of the SigB-dependent general stress regulon of Bacillus subtilis during growth at high temperature.
J Bacteriol: 2004, 186(18);6150-8
[PubMed:15342585] [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)

A Petersohn, M Brigulla, S Haas, J D Hoheisel, U Völker, M Hecker
Global analysis of the general stress response of Bacillus subtilis.
J Bacteriol: 2001, 183(19);5617-31
[PubMed:11544224] [WorldCat.org] [DOI] (P p)

U Voelker, A Voelker, W G Haldenwang
The yeast two-hybrid system detects interactions between Bacillus subtilis sigmaB regulators.
J Bacteriol: 1996, 178(23);7020-3
[PubMed:8955331] [WorldCat.org] [DOI] (P p)

X Yang, C M Kang, M S Brody, C W Price
Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor.
Genes Dev: 1996, 10(18);2265-75
[PubMed:8824586] [WorldCat.org] [DOI] (P p)

U Voelker, A Voelker, W G Haldenwang
Reactivation of the Bacillus subtilis anti-sigma B antagonist, RsbV, by stress- or starvation-induced phosphatase activities.
J Bacteriol: 1996, 178(18);5456-63
[PubMed:8808936] [WorldCat.org] [DOI] (P p)

S Alper, A Dufour, D A Garsin, L Duncan, R Losick
Role of adenosine nucleotides in the regulation of a stress-response transcription factor in Bacillus subtilis.
J Mol Biol: 1996, 260(2);165-77
[PubMed:8764398] [WorldCat.org] [DOI] (P p)

C M Kang, M S Brody, S Akbar, X Yang, C W Price
Homologous pairs of regulatory proteins control activity of Bacillus subtilis transcription factor sigma(b) in response to environmental stress.
J Bacteriol: 1996, 178(13);3846-53
[PubMed:8682789] [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 Dufour, W G Haldenwang
Interactions between a Bacillus subtilis anti-sigma factor (RsbW) and its antagonist (RsbV).
J Bacteriol: 1994, 176(7);1813-20
[PubMed:8144446] [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)