Difference between revisions of "RsbT"

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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:'''  
+
* '''Catalyzed reaction/ biological activity:''' ATP + a protein = ADP + a phosphoprotein (according to Swiss-Prot)
  
 
* '''Protein family:'''
 
* '''Protein family:'''

Revision as of 12:34, 23 May 2009

  • Description: PP2C activator, protein serine kinase, phosphorylates RsbS, part of the stressosome

Gene name rsbT
Synonyms ycxT
Essential no
Product PP2C activator, protein serine kinase
Function control of SigB activity
MW, pI 14 kDa, 6.587
Gene length, protein length 399 bp, 133 aa
Immediate neighbours rsbS, rsbU
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RsbT context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + a protein = ADP + a phosphoprotein (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • Structure: 3VY9 (complete stressosome)
  • E.C. number:

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

Your additional remarks

References

  1. Marles-Wright, J., Grant, T., Delumeau, O., van Duinen, G., Firbank, S. J., Lewis, P. J., Murray, J. W., Newman, J. A., Quin, M. B., Race, P. R., Rohou, A., Tichelaar, W., van Heel, M. & Lewis, R. J. (2008) Molecular architecture of the "stressosome," a signal integration and transduction hub. Science 322: 92-96. PubMed
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed