PrkC

• Description: protein kinase C
  
  

Gene name	prkC
Synonyms	yloP
Essential	no
Product	protein kinase
Function	germination in response to muropeptides
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU15770

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

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on Thr-290 PubMed

• Cofactor(s):

• Effectors of protein activity: activated by muropeptides PubMed

• Interactions:

• Localization: membrane (according to Swiss-Prot), membrane PubMed

Database entries

• Structure:

• Swiss prot entry: O34507

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: prpC-prkC-cpgA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector: pGP832 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P 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)

1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed