RsbX

• Description: protein serine phosphatase, feedback PP2C, dephosphorylates RsbS
  
  

Gene name	rsbX
Synonyms
Essential	no
Product	protein serine phosphatase, feedback PP2C
Function	control of SigB activity
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	21 kDa, 6.23
Gene length, protein length	597 bp, 199 aa
Immediate neighbours	sigB, ydcF
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU04740

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: dephosphorylation of RsbS-P

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P17906

• KEGG entry: [3]

• E.C. number: 3.1.3.3

Expression and regulation

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

Masatoshi Suganuma, Aik Hong Teh, Masatomo Makino, Nobutaka Shimizu, Tomonori Kaneko, Kunio Hirata, Masaki Yamamoto, Takashi Kumasaka
Crystallization and preliminary X-ray analysis of the stress-response PPM phosphatase RsbX from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 11);1128-30
[PubMed:19923733] [WorldCat.org] [DOI] (I 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)

J M Scott, T Mitchell, W G Haldenwang
Stress triggers a process that limits activation of the Bacillus subtilis stress transcription factor sigma(B).
J Bacteriol: 2000, 182(5);1452-6
[PubMed:10671474] [WorldCat.org] [DOI] (P p)

N Smirnova, J Scott, U Voelker, W G Haldenwang
Isolation and characterization of Bacillus subtilis sigB operon mutations that suppress the loss of the negative regulator RsbX.
J Bacteriol: 1998, 180(14);3671-80
[PubMed:9658013] [WorldCat.org] [DOI] (P p)

U Voelker, T Luo, N Smirnova, W Haldenwang
Stress activation of Bacillus subtilis sigma B can occur in the absence of the sigma B negative regulator RsbX.
J Bacteriol: 1997, 179(6);1980-4
[PubMed:9068644] [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)

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)

U Voelker, A Dufour, W G Haldenwang
The Bacillus subtilis rsbU gene product is necessary for RsbX-dependent regulation of sigma B.
J Bacteriol: 1995, 177(1);114-22
[PubMed:8002609] [WorldCat.org] [DOI] (P p)