Difference between revisions of "RsbRD"

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=References=
 
=References=
  
<pubmed>15312768,10482513 ,20019076,17726680 17218307, 20935101 </pubmed>
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<pubmed>15312768,10482513 ,20019076,17726680 17218307, </pubmed>
 
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'''Additional publications:''' {{PubMed|20935101}}
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:56, 12 October 2010

  • Description: probably part of the stressosome, negative regulator of SigB activity

Gene name rsbRD
Synonyms yqhA
Essential no
Product RsbR paralog
Function control of SigB activity
MW, pI 31 kDa, 5.089
Gene length, protein length 834 bp, 278 aa
Immediate neighbours yqhB, trnSL-Gln1
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YqhA context.gif
This image was kindly provided by SubtiList





The gene

Basic information

  • Locus tag: BSU24760

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: rsbRD (according to DBTBS)
  • 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

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)

A Petersohn, J Bernhardt, U Gerth, D Höper, T Koburger, U Völker, M Hecker
Identification of sigma(B)-dependent genes in Bacillus subtilis using a promoter consensus-directed search and oligonucleotide hybridization.
J Bacteriol: 1999, 181(18);5718-24
[PubMed:10482513] [WorldCat.org] [DOI] (P p)

Additional publications: PubMed