RsbP
- Description: protein serine phosphatase, energy PP2C, dephosphorylates RsbV
Gene name | rsbP |
Synonyms | yvfP |
Essential | no |
Product | protein serine phosphatase, energy PP2C |
Function | control of SigB activity |
Metabolic function and regulation of this protein in SubtiPathways: Stress | |
MW, pI | 45 kDa, 4.827 |
Gene length, protein length | 1209 bp, 403 aa |
Immediate neighbours | rsbQ, yvfO |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU34110
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains: N-terminal PAS domain, central coiled-coil domain, C-terminal PP2C phosphatase domain
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- Swiss prot entry: O07014
- KEGG entry: [2]
- E.C. number: 3.1.3.3
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Chet Price, Davis, USA homepage
Your additional remarks
References
Masatomo Makino, Shinpei Kondo, Tomonori Kaneko, Seiki Baba, Kunio Hirata, Takashi Kumasaka
Expression, crystallization and preliminary crystallographic analysis of the PAS domain of RsbP, a stress-response phosphatase from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 6);559-61
[PubMed:19478430]
[WorldCat.org]
[DOI]
(I p)
Margaret S Brody, Valley Stewart, Chester W Price
Bypass suppression analysis maps the signalling pathway within a multidomain protein: the RsbP energy stress phosphatase 2C from Bacillus subtilis.
Mol Microbiol: 2009, 72(5);1221-34
[PubMed:19432806]
[WorldCat.org]
[DOI]
(I p)
Shuyu Zhang, W G Haldenwang
Contributions of ATP, GTP, and redox state to nutritional stress activation of the Bacillus subtilis sigmaB transcription factor.
J Bacteriol: 2005, 187(22);7554-60
[PubMed:16267279]
[WorldCat.org]
[DOI]
(P p)
Tomonori Kaneko, Nobuo Tanaka, Takashi Kumasaka
Crystal structures of RsbQ, a stress-response regulator in Bacillus subtilis.
Protein Sci: 2005, 14(2);558-65
[PubMed:15632289]
[WorldCat.org]
[DOI]
(P 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)
Matthias Brigulla, Tamara Hoffmann, Andrea Krisp, Andrea Völker, Erhard Bremer, Uwe Völker
Chill induction of the SigB-dependent general stress response in Bacillus subtilis and its contribution to low-temperature adaptation.
J Bacteriol: 2003, 185(15);4305-14
[PubMed:12867438]
[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)
K Vijay, M S Brody, E Fredlund, C W Price
A PP2C phosphatase containing a PAS domain is required to convey signals of energy stress to the sigmaB transcription factor of Bacillus subtilis.
Mol Microbiol: 2000, 35(1);180-8
[PubMed:10632888]
[WorldCat.org]
[DOI]
(P p)