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, GpsB PubMed

Extended information on the protein

  • Kinetic information:
  • 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
    • 4X3F (intracellular domain of the Mycobacterium tuberculosis enzyme, 36% identity, 68% similarity) 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

Sandro F F Pereira, Lindsie Goss, Jonathan Dworkin
Eukaryote-like serine/threonine kinases and phosphatases in bacteria.
Microbiol Mol Biol Rev: 2011, 75(1);192-212
[PubMed:21372323] [WorldCat.org] [DOI] (I p)

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

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


Phsiological role of PrkC

Expression of PrkC

Yan Chen, W Keith Ray, Richard F Helm, Stephen B Melville, David L Popham
Levels of germination proteins in Bacillus subtilis dormant, superdormant, and germinating spores.
PLoS One: 2014, 9(4);e95781
[PubMed:24752279] [WorldCat.org] [DOI] (I e)

Adam Iwanicki, Krzysztof Hinc, Simone Seror, Grzegorz Wegrzyn, Michal Obuchowski
Transcription in the prpC-yloQ region in Bacillus subtilis.
Arch Microbiol: 2005, 183(6);421-30
[PubMed:16025310] [WorldCat.org] [DOI] (P p)

Structure/ biochemistry of PrkC

Rita Berisio, Flavia Squeglia, Alessia Ruggiero, Luigi Petraccone, Marco Ignazio Stellato, Pompea Del Vecchio
Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies.
Biochim Biophys Acta: 2015, 1854(5);402-9
[PubMed:25668224] [WorldCat.org] [DOI] (P p)

Tristan Wagner, Matthieu Alexandre, Rosario Duran, Nathalie Barilone, Annemarie Wehenkel, Pedro M Alzari, Marco Bellinzoni
The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation.
Proteins: 2015, 83(5);982-8
[PubMed:25586004] [WorldCat.org] [DOI] (I p)

Gunjan Arora, Andaleeb Sajid, Mary Diana Arulanandh, Richa Misra, Anshika Singhal, Santosh Kumar, Lalit K Singh, Abid R Mattoo, Rishi Raj, Souvik Maiti, Sharmila Basu-Modak, Yogendra Singh
Zinc regulates the activity of kinase-phosphatase pair (BasPrkC/BasPrpC) in Bacillus anthracis.
Biometals: 2013, 26(5);715-30
[PubMed:23793375] [WorldCat.org] [DOI] (I p)

Flavia Squeglia, Roberta Marchetti, Alessia Ruggiero, Rosa Lanzetta, Daniela Marasco, Jonathan Dworkin, Maxim Petoukhov, Antonio Molinaro, Rita Berisio, Alba Silipo
Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy.
J Am Chem Soc: 2011, 133(51);20676-9
[PubMed:22111897] [WorldCat.org] [DOI] (I p)

Alessia Ruggiero, Flavia Squeglia, Daniela Marasco, Roberta Marchetti, Antonio Molinaro, Rita Berisio
X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus.
Biochem J: 2011, 435(1);33-41
[PubMed:21208192] [WorldCat.org] [DOI] (I p)