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
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 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
• reduced growth at high salt PubMed

Database entries

• BsubCyc: BSU15770

• 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, YvcK PubMed, GpsB PubMed

Extended information on the protein

• Kinetic information:

• Domains:
  • contains three C-terminal PASTA domains (aa 356-424, 425-492, 493-559) (binds muropeptides) PubMed

• Modification: phosphorylation on Thr-290 PubMed, autophosphorylation on multiple threonine residues PubMed

• Cofactors:

• Effectors of protein activity:
  • activated by muropeptides PubMed
  • GpsB, DivIVA, and EzrA are required for stimulation of PrkC activity PubMed

• Interactions:
  • AbrB-PrkC PubMed
  • YvcK-PrkC PubMed
  • GpsB-PrkC PubMed

• Localization:
  • inner spore membrane PubMed
  • membrane PubMed
  • division septum PubMed

Database entries

• BsubCyc: BSU15770

• 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

• 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

Targets of PrkC-dependent phosphorylation

Frédérique Pompeo, Elodie Foulquier, Bastien Serrano, Christophe Grangeasse, Anne Galinier
Phosphorylation of the cell division protein GpsB regulates PrkC kinase activity through a negative feedback loop in Bacillus subtilis.
Mol Microbiol: 2015, 97(1);139-50
[PubMed:25845974] [WorldCat.org] [DOI] (I p)

Lei Shi, Nathalie Pigeonneau, Vaishnavi Ravikumar, Paula Dobrinic, Boris Macek, Damjan Franjevic, Marie-Francoise Noirot-Gros, Ivan Mijakovic
Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues.
Front Microbiol: 2014, 5;495
[PubMed:25278935] [WorldCat.org] [DOI] (P e)

Elodie Foulquier, Frédérique Pompeo, Céline Freton, Baptiste Cordier, Christophe Grangeasse, Anne Galinier
PrkC-mediated phosphorylation of overexpressed YvcK protein regulates PBP1 protein localization in Bacillus subtilis mreB mutant cells.
J Biol Chem: 2014, 289(34);23662-9
[PubMed:25012659] [WorldCat.org] [DOI] (I p)

Ahasanul Kobir, Sandrine Poncet, Vladimir Bidnenko, Olivier Delumeau, Carsten Jers, Samira Zouhir, Rosa Grenha, Sylvie Nessler, Phillipe Noirot, Ivan Mijakovic
Phosphorylation of Bacillus subtilis gene regulator AbrB modulates its DNA-binding properties.
Mol Microbiol: 2014, 92(5);1129-41
[PubMed:24731262] [WorldCat.org] [DOI] (I p)

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)

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)