Difference between revisions of "PrkC"
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* '''Mutant:''' GP576 (spc), OMG302 (aphA3), available in [[Stülke]] lab | * '''Mutant:''' GP576 (spc), OMG302 (aphA3), available in [[Stülke]] lab | ||
** 1A820 ( ''prkC''::''erm''), {{PubMed|12682299}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A820&Search=1A820 BGSC] | ** 1A820 ( ''prkC''::''erm''), {{PubMed|12682299}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A820&Search=1A820 BGSC] | ||
+ | ** 1A963 (no resistance), {{PubMed|12399479}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A963&Search=1A963 BGSC] | ||
* '''Expression vector:''' | * '''Expression vector:''' |
Revision as of 10:43, 20 September 2012
- 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 |
Get the DNA and protein sequences (Barbe et al., 2009) | |
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
- 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
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
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
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)
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)
Expression of PrkC: PubMed
Structure/ biochemistry of PrkC
Flavia Squeglia, Roberta Marchetti, Alessia Ruggiero, Rosa Lanzetta, Daniela Marasco, Jonathan Dworkin, Maxim Petoukhov, Antonio Molinaro, Rita Berisio, Alba Silipo
Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy.
J Am Chem Soc: 2011, 133(51);20676-9
[PubMed:22111897]
[WorldCat.org]
[DOI]
(I p)
Alessia Ruggiero, Flavia Squeglia, Daniela Marasco, Roberta Marchetti, Antonio Molinaro, Rita Berisio
X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus.
Biochem J: 2011, 435(1);33-41
[PubMed:21208192]
[WorldCat.org]
[DOI]
(I p)