PrkC

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  • Description: protein kinase C, induce germination of spores in response to DAP-type, and not to Lys-type cell wall muropeptides

Gene name prkC
Synonyms yloP
Essential no
Product protein kinase
Function germination in response to muropeptides
Gene expression levels in SubtiExpress: prkC
Interactions involving this protein in SubtInteract: PrkC
Metabolic function and regulation of this protein in SubtiPathways:
prkC
MW, pI 71 kDa, 4.833
Gene length, protein length 1944 bp, 648 aa
Immediate neighbours prpC, cpgA
Sequences Protein DNA DNA_with_flanks
Genetic context
PrkC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PrkC expression.png















Categories containing this gene/protein

protein modification, germination, membrane proteins, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU15770

Phenotypes of a mutant

  • unable to germinate in response to muropeptides PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

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

Proteins phosphorylated by PrkC

CpgA, EF-Tu, YezB PubMed, EF-G PubMed, YwjH, GlnA, Icd, AlsD, HPr PubMed, YkwC PubMed, YvcK PubMed

Extended information on the protein

  • Kinetic information:
  • Domains: PASTA domain at the C-terminus (binds muropeptides) PubMed
  • Modification: phosphorylation on Thr-290 PubMed, autophosphorylation on multiple threonine residues PubMed
  • Effectors of protein activity: activated by muropeptides PubMed

Database entries

  • Structure: 3PY3 (entire extra-cellular region of PrkC from Staphylococcus aureus) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP576 (spc), OMG302 (aphA3), available in Stülke lab
  • Expression vector:
    • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP832, available in Stülke lab
    • for expression/ purification of the kinase domain from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP849, available in Stülke lab
    • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP1001, available in Stülke lab
    • for expression, purification in E. coli with N-terminal Strep-tag, in pGP172: pGP825, available in Stülke lab
  • lacZ fusion: pGP829 (in pAC7), available in Stülke lab
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews


Phosphorylation of PrkC

Targets of PrkC-dependent phosphorylation

Phsiological role of PrkC

Cédric Absalon, Michal Obuchowski, Edwige Madec, Delphine Delattre, I Barry Holland, Simone J Séror
CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis.
Microbiology (Reading): 2009, 155(Pt 3);932-943
[PubMed:19246764] [WorldCat.org] [DOI] (P p)

Ishita M Shah, Maria-Halima Laaberki, David L Popham, Jonathan Dworkin
A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments.
Cell: 2008, 135(3);486-96
[PubMed:18984160] [WorldCat.org] [DOI] (I p)

Edwige Madec, Allan Stensballe, Sven Kjellström, Lionel Cladière, Michal Obuchowski, Ole Nørregaard Jensen, Simone J Séror
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: 2003, 330(3);459-72
[PubMed:12842463] [WorldCat.org] [DOI] (P p)

Edwige Madec, Agnieszka Laszkiewicz, Adam Iwanicki, Michal Obuchowski, Simone Séror
Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes.
Mol Microbiol: 2002, 46(2);571-86
[PubMed:12406230] [WorldCat.org] [DOI] (P p)

Tatiana A Gaidenko, Tae-Jong Kim, Chester W Price
The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells.
J Bacteriol: 2002, 184(22);6109-14
[PubMed:12399479] [WorldCat.org] [DOI] (P p)

Expression of PrkC

Structure/ biochemistry of PrkC