Difference between revisions of "PrkC"
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=References= | =References= | ||
+ | ==Reviews== | ||
+ | <pubmed> 20972452 </pubmed> | ||
==Phosphorylation of PrkC== | ==Phosphorylation of PrkC== | ||
− | <pubmed>12842463 | + | <pubmed>12842463 </pubmed> |
+ | '''Additional publications: ''' {{PubMed|20563625}} | ||
==Targets of PrkC-dependent phosphorylation== | ==Targets of PrkC-dependent phosphorylation== | ||
<pubmed>19246764, 20070526 ,20389117 </pubmed> | <pubmed>19246764, 20070526 ,20389117 </pubmed> | ||
==Phsiological role of PrkC== | ==Phsiological role of PrkC== | ||
<pubmed>12399479, 12406230, 19246764, 12842463 , 18984160 </pubmed> | <pubmed>12399479, 12406230, 19246764, 12842463 , 18984160 </pubmed> | ||
− | ==Expression of PrkC== | + | ==Expression of PrkC: {{PubMed|16025310}}== |
− | + | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:16, 26 October 2010
- 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
|
Contents
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)
- 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
Extended information on the protein
- Kinetic information:
- Domains: PASTA domain at the C-terminus (binds muropeptides) PubMed
- Modification: phosphorylation on Thr-290 PubMed, autophosphorylation on multiple threonine residues PubMed
- Cofactor(s):
- Effectors of protein activity: activated by muropeptides PubMed
- Interactions:
Database entries
- Structure:
- UniProt: O34507
- KEGG entry: [2]
- E.C. number: 2.7.11.1
Additional information
Expression and regulation
- Sigma factor:
- 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
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
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)
Additional publications: PubMed
Targets of PrkC-dependent phosphorylation
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