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
| |
Contents
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
- BsubCyc: BSU15770
- 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)
- 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
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
- Effectors of protein activity: activated by muropeptides PubMed
- Localization: inner spore membrane PubMed, membrane PubMed
Database entries
- BsubCyc: BSU15770
- Structure:
- UniProt: O34507
- KEGG entry: [2]
- E.C. number: 2.7.11.1
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
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Phosphorylation of PrkC
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)
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
