Difference between revisions of "RsbU"

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* '''Description:''' [[Protein kinases and phosphatases|protein serine phosphatase]], environmental PP2C, dephosphorylates [[RsbV]] <br/><br/>
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|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity
 
|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU04700 rsbU]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/RsbU RsbU]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/RsbU RsbU]

Revision as of 15:19, 6 August 2012


Gene name rsbU
Synonyms
Essential no
Product protein serine phosphatase, environmental PP2C
Function control of SigB activity
Gene expression levels in SubtiExpress: rsbU
Interactions involving this protein in SubtInteract: RsbU
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 38 kDa, 4.906
Gene length, protein length 1005 bp, 335 aa
Immediate neighbours rsbT, rsbV
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RsbU context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RsbU expression.png




























Categories containing this gene/protein

protein modification, sigma factors and their control

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU04700

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

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:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Jon Marles-Wright, Richard J Lewis
The stressosome: molecular architecture of a signalling hub.
Biochem Soc Trans: 2010, 38(4);928-33
[PubMed:20658979] [WorldCat.org] [DOI] (I p)

Original publications

Steven W Hardwick, Jan Pané-Farré, Olivier Delumeau, Jon Marles-Wright, James W Murray, Michael Hecker, Richard J Lewis
Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.
J Biol Chem: 2007, 282(15);11562-72
[PubMed:17303566] [WorldCat.org] [DOI] (P p)

Shuyu Zhang, Adam Reeves, Robyn L Woodbury, W G Haldenwang
Coexpression patterns of sigma(B) regulators in Bacillus subtilis affect sigma(B) inducibility.
J Bacteriol: 2005, 187(24);8520-5
[PubMed:16321960] [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)

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)

Chien-Cheng Chen, Richard J Lewis, Robin Harris, Michael D Yudkin, Olivier Delumeau
A supramolecular complex in the environmental stress signalling pathway of Bacillus subtilis.
Mol Microbiol: 2003, 49(6);1657-69
[PubMed:12950928] [WorldCat.org] [DOI] (P p)

Emmanuel Guedon, Charles M Moore, Qiang Que, Tao Wang, Rick W Ye, John D Helmann
The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and sigmaB regulons.
Mol Microbiol: 2003, 49(6);1477-91
[PubMed:12950915] [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)

Sujit Dutta, Richard J Lewis
Crystallization and preliminary crystallographic analysis of the kinase-recruitment domain of the PP2C-type phosphatase RsbU.
Acta Crystallogr D Biol Crystallogr: 2003, 59(Pt 1);191-3
[PubMed:12499568] [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)

C M Kang, K Vijay, C W Price
Serine kinase activity of a Bacillus subtilis switch protein is required to transduce environmental stress signals but not to activate its target PP2C phosphatase.
Mol Microbiol: 1998, 30(1);189-96
[PubMed:9786195] [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, 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)

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)

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)