PrkC

• 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
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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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: 3PY3 (entire extra-cellular region of PrkC from Staphylococcus aureus) PubMed

• UniProt: O34507

• KEGG entry: [2]

• E.C. number: 2.7.11.1

Expression and regulation

• Operon: prpC-prkC-cpgA PubMed

• Expression browser: prkC PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: GP576 (spc), OMG302 (aphA3), available in Stülke lab
  • 1A820 ( prkC::erm), PubMed, available at BGSC
  • 1A963 (no resistance), PubMed, available at BGSC
  • 1A964 (no resistance), PubMed, available at BGSC

• 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

Phosphorylation of PrkC

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)

Additional publications: PubMed

Targets of PrkC-dependent phosphorylation

Nico Pietack, Dörte Becher, Sebastian R Schmidl, Milton H Saier, Michael Hecker, Fabian M Commichau, Jörg Stülke
In vitro phosphorylation of key metabolic enzymes from Bacillus subtilis: PrkC phosphorylates enzymes from different branches of basic metabolism.
J Mol Microbiol Biotechnol: 2010, 18(3);129-40
[PubMed:20389117] [WorldCat.org] [DOI] (I p)

Ishita M Shah, Jonathan Dworkin
Induction and regulation of a secreted peptidoglycan hydrolase by a membrane Ser/Thr kinase that detects muropeptides.
Mol Microbiol: 2010, 75(5);1232-43
[PubMed:20070526] [WorldCat.org] [DOI] (I p)

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)