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: 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 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, YkwC 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

• Cofactors:

• 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

Paweł Gruszczyński, Michał Obuchowski, Rajmund Kaźmierkiewicz
Phosphorylation and ATP-binding induced conformational changes in the PrkC, Ser/Thr kinase from B. subtilis.
J Comput Aided Mol Des: 2010, 24(9);733-47
[PubMed:20563625] [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)

Targets of PrkC-dependent phosphorylation

Vaishnavi Ravikumar, Lei Shi, Karsten Krug, Abderahmane Derouiche, Carsten Jers, Charlotte Cousin, Ahasanul Kobir, Ivan Mijakovic, Boris Macek
Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC.
Mol Cell Proteomics: 2014, 13(8);1965-78
[PubMed:24390483] [WorldCat.org] [DOI] (I p)

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)

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)