Difference between revisions of "PrkC"

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(Proteins phosphorylated by PrkC)
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The 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}}, [[YkwC]] 24390483
+
[[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}}, [[YkwC]] {{PubMed|24390483}}
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:''' PASTA domain at the C-terminus (binds muropeptides) {{PubMed|18984160}}  
+
* '''[[Domains]]:''' PASTA domain at the C-terminus (binds muropeptides) {{PubMed|18984160}}  
  
 
* '''Modification:''' phosphorylation on Thr-290 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], autophosphorylation on multiple threonine residues {{PubMed|12842463,20389117}}
 
* '''Modification:''' phosphorylation on Thr-290 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], autophosphorylation on multiple threonine residues {{PubMed|12842463,20389117}}
  
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:''' activated by muropeptides {{PubMed|18984160}}  
 
* '''Effectors of protein activity:''' activated by muropeptides {{PubMed|18984160}}  
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<pubmed>12842463 20563625</pubmed>
 
<pubmed>12842463 20563625</pubmed>
 
==Targets of PrkC-dependent phosphorylation==
 
==Targets of PrkC-dependent phosphorylation==
<pubmed>19246764, 20070526 ,20389117 </pubmed>
+
<pubmed>19246764, 20070526 ,20389117 24390483</pubmed>
 
==Phsiological role of PrkC==
 
==Phsiological role of PrkC==
 
<pubmed>12399479, 12406230, 19246764,  12842463 , 18984160 </pubmed>
 
<pubmed>12399479, 12406230, 19246764,  12842463 , 18984160 </pubmed>

Revision as of 13:23, 7 January 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
PrkC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PrkC expression.png















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)
  • 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:
  • Domains: PASTA domain at the C-terminus (binds muropeptides) PubMed
  • Modification: phosphorylation on Thr-290 PubMed, autophosphorylation on multiple threonine residues PubMed
  • Effectors of protein activity: activated by muropeptides PubMed

Database entries

  • Structure: 3PY3 (entire extra-cellular region of PrkC from Staphylococcus aureus) PubMed
  • KEGG entry: [2]

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
  • 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

Reviews


Phosphorylation of PrkC

Targets of PrkC-dependent phosphorylation

Phsiological role of PrkC

Expression of PrkC

Structure/ biochemistry of PrkC

Gunjan Arora, Andaleeb Sajid, Mary Diana Arulanandh, Richa Misra, Anshika Singhal, Santosh Kumar, Lalit K Singh, Abid R Mattoo, Rishi Raj, Souvik Maiti, Sharmila Basu-Modak, Yogendra Singh
Zinc regulates the activity of kinase-phosphatase pair (BasPrkC/BasPrpC) in Bacillus anthracis.
Biometals: 2013, 26(5);715-30
[PubMed:23793375] [WorldCat.org] [DOI] (I p)

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)