PrkC

From SubtiWiki
Revision as of 14:12, 15 March 2009 by Jstuelk (talk | contribs) (Proteins phosphorylated by PrkC)
Jump to: navigation, search
  • Description: protein kinase C

Gene name prkC
Synonyms yloP
Essential no
Product protein kinase
Function germination in response to muropeptides
MW, pI 71 kDa, 4.833
Gene length, protein length 1944 bp, 648 aa
Immediate neighbours prpC, cpgA
Gene sequence (+200bp) Protein sequence
Genetic context
PrkC context.gif



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Proteins phosphorylated by PrkC

CpgA, EF-Tu, YezB PubMed, EF-G PubMed

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: activated by muropeptides PubMed
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry:
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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. Gaidenko TA, Kim TJ, Price CW: (2002) The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J Bacteriol, 184:6109-6114. PubMed
  2. Madec E, Laszkiewicz A, Iwanicki A, Obuchowski M, Séror S: (2002) Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes. Mol Microbiol, 46:571-586. PubMed
  3. Madec E, Stensballe A, Kjellström S, Cladière L, Obuchowski M, Jensen ON, Séror S: (2003) Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis. J Mol Biol 330:459-472. PubMed
  4. Shah IM, Laaberki MH, Popham DL, Dworkin J: A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 2008, 135:486-496. PubMed
  5. Absalon C, Obuchowski M, Madec E, Delattre D, Holland IB, Séror SJ (2009) CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology 155: 932-943. PubMed
  6. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed