Difference between revisions of "RsbRB"

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* '''Operon:'''  
 
* '''Operon:'''  
  
* '''[[Sigma factor]]:'''  
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rsbRB_1387206_1388039_1 rsbRB] {{PubMed|22383849}}
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* '''Sigma factor:'''  
  
 
* '''Regulation:''' constitutively expressed {{PubMed|20019076}}  
 
* '''Regulation:''' constitutively expressed {{PubMed|20019076}}  

Revision as of 07:30, 13 April 2012

Gene name rsbRB
Synonyms ispU, ykoB
Essential no
Product RsbR paralog
Function control of SigB activity
Interactions involving this protein in SubtInteract: RsbRB
MW, pI 32 kDa, 4.788
Gene length, protein length 831 bp, 277 aa
Immediate neighbours ispA, thiX
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YkoB context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

sigma factors and their control, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU13200

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • negative regulator of YtvA-dependent light activation of the SigB stress response PubMed
  • Protein family:

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Thr-186 and probably also on Thr-220 by RsbT PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation: constitutively expressed PubMed
  • 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

Additional publications: PubMed

Adam Reeves, Luis Martinez, William Haldenwang
Expression of, and in vivo stressosome formation by, single members of the RsbR protein family in Bacillus subtilis.
Microbiology (Reading): 2010, 156(Pt 4);990-998
[PubMed:20019076] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [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)