PrkC

• Description: protein kinase C
  
  

Gene name	prkC
Synonyms	yloP
Essential	no
Product	protein kinase
Function	germination in response to muropeptides
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	71 kDa, 4.833
Gene length, protein length	1944 bp, 648 aa
Immediate neighbours	prpC, cpgA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

protein modification, germination, membrane proteins, phosphoproteins

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]

The protein

Basic information/ Evolution

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

• Protein family: protein kinase domain (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

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

• Cofactor(s):

• Effectors of protein activity: activated by muropeptides PubMed

• Interactions:

• Localization: inner spore membrane PubMed, membrane PubMed

Database entries

• Structure:

• UniProt: O34507

• KEGG entry: [2]

• E.C. number: 2.7.11.1

Expression and regulation

• Operon: prpC-prkC-cpgA PubMed

• Sigma factor:

• 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:

References

Reviews

Jonathan Dworkin, Ishita M Shah
Exit from dormancy in microbial organisms.
Nat Rev Microbiol: 2010, 8(12);890-6
[PubMed:20972452] [WorldCat.org] [DOI] (I p)

Phosphorylation of PrkC

Additional publications: PubMed

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)