Difference between revisions of "PrkC"
| Line 58: | Line 58: | ||
| === Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15770&redirect=T BSU15770] | ||
| * '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
| Line 96: | Line 97: | ||
| === Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15770&redirect=T BSU15770] | ||
| * '''Structure:''' [http://www.rcsb.org/pdb/search/structidSearch.do?structureId=3PY9 3PY3] (entire extra-cellular region of PrkC from ''Staphylococcus aureus'')  {{PubMed|21208192}}   | * '''Structure:''' [http://www.rcsb.org/pdb/search/structidSearch.do?structureId=3PY9 3PY3] (entire extra-cellular region of PrkC from ''Staphylococcus aureus'')  {{PubMed|21208192}}   | ||
Revision as of 13:41, 2 April 2014
-  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   | |
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
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
- Localization: inner spore membrane PubMed, membrane PubMed
Database entries
- BsubCyc: BSU15770
- 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
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
Structure/ biochemistry of PrkC

