Difference between revisions of "PrkC"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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=== Proteins phosphorylated by PrkC === | === Proteins phosphorylated by PrkC === | ||
− | [[CpgA]], [[tufA | EF-Tu]], [[YezB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/19246764 PubMed], [[fusA | EF-G]] [http://www.ncbi.nlm.nih.gov/sites/entrez/18984160 PubMed], [[YwjH]], [[GlnA]], [[Icd]], [[AlsD]], [[ptsH|HPr]] {{PubMed|20389117}} | + | [[CpgA]], [[tufA|EF-Tu]], [[YezB]] [http://www.ncbi.nlm.nih.gov/sites/entrez/19246764 PubMed], [[fusA|EF-G]] [http://www.ncbi.nlm.nih.gov/sites/entrez/18984160 PubMed], [[YwjH]], [[GlnA]], [[Icd]], [[AlsD]], [[ptsH|HPr]] {{PubMed|20389117}} |
=== Extended information on the protein === | === Extended information on the protein === | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=prkC_1651142_1653088_1 prkC] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=prkC_1651142_1653088_1 prkC] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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==Phosphorylation of PrkC== | ==Phosphorylation of PrkC== | ||
− | <pubmed>12842463 </pubmed> | + | <pubmed>12842463 20563625</pubmed> |
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==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</pubmed> | ||
==Structure/ biochemistry of PrkC== | ==Structure/ biochemistry of PrkC== | ||
− | <pubmed> 21208192 22111897 </pubmed> | + | <pubmed> 21208192 22111897 23793375 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:29, 1 July 2013
- 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: Central C-metabolism | |
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
- 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
- Localization: inner spore membrane PubMed, membrane PubMed
Database entries
- 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
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
Structure/ biochemistry of PrkC