Difference between revisions of "PrkC"

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(References)
(Database entries)
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* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU15770]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU15770]
  
* '''E.C. number:'''
+
* '''E.C. number:'''[http://www.expasy.org/enzyme/2.7.11.1 2.7.11.1]
  
 
=== Additional information===
 
=== Additional information===

Revision as of 08:27, 4 August 2010

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
PrkC context.gif
This image was kindly provided by SubtiList







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)
  • 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:
  • KEGG entry: [2]

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
  • lacZ fusion: pGP829 (in pAC7), available in Stülke lab
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

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

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, Engl.): 2009, 155(Pt 3);932-43
[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, Engl.): 2009, 155(Pt 3);932-43
[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

Adam Iwanicki, Krzysztof Hinc, Simone Seror, Grzegorz Wegrzyn, Michal Obuchowski
Transcription in the prpC-yloQ region in Bacillus subtilis.
Arch. Microbiol.: 2005, 183(6);421-30
[PubMed:16025310] [WorldCat.org] [DOI] (P p)