Difference between revisions of "RsbRD"

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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/BSU24760 rsbRD]
 
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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/RsbRD RsbRD]
 
|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/RsbRD RsbRD]

Revision as of 11:41, 7 August 2012

  • 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
Gene expression levels in SubtiExpress: rsbRD
Interactions involving this protein in SubtInteract: RsbRD
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
Expression at a glance   PubMed
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Categories containing this gene/protein

sigma factors and their control, general stress proteins (controlled by SigB), membrane proteins, phosphoproteins

This gene is a member of the following regulons

SigB regulon

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:
  • Modification: phosphorylation on Thr-181 by RsbT PubMed
  • Cofactor(s):
  • Effectors of protein activity:

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

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)

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)