Difference between revisions of "Sandbox"

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* '''Description:''' protein kinase C <br/><br/>
+
* '''Description:''' protein phosphatase <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
−
|''prkC''
+
|''prpC''
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yloP ''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yloO ''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Product''' || protein kinase
+
|style="background:#ABCDEF;" align="center"| '''Product''' || protein phosphatase
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Function''' || germination in response to muropeptides
+
|style="background:#ABCDEF;" align="center"|'''Function''' || antagonist of PrkC-dependent phosphorylation
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 71 kDa, 4.833  
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 27 kDa, 4.355  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1944 bp, 648 aa  
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 762 bp, 254 aa  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[prpC]]'', ''[[cpgA]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yloN]]'', ''[[prkC]]''
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Hier soll was neues rein'''
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Hier soll was neues rein'''
 
|-
 
|-
−
|colspan="2" | '''Genetic context''' <br/> [[Image:prkC_context.gif]]
+
|colspan="2" | '''Genetic context''' <br/> [[Image:prpC_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
Line 43: Line 43:
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
  
−
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG13391]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG13390]
  
 
=== Additional information===
 
=== Additional information===
Line 58: Line 58:
 
* '''Paralogous protein(s):'''
 
* '''Paralogous protein(s):'''
  
−
=== Proteins phosphorylated by PrkC ===
+
=== Proteins dephosphorylated by PrpC ===
  
−
[[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]
+
[[CpgA]],  [[tufA | EF-Tu]], [[YezB]]  [http://www.ncbi.nlm.nih.gov/sites/entrez/19246764 PubMed], [[ptsH | HPr]] [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537  PubMed]
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
Line 68: Line 68:
 
* '''Domains:'''  
 
* '''Domains:'''  
  
−
* '''Modification:''' phosphorylation on Thr-290 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
+
* '''Modification:'''
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
−
* '''Effectors of protein activity:''' activated by muropeptides [http://www.ncbi.nlm.nih.gov/sites/entrez/18984160 PubMed]
+
* '''Effectors of protein activity:'''
  
 
* '''Interactions:'''
 
* '''Interactions:'''
  
−
* '''Localization:''' membrane [http://www.ncbi.nlm.nih.gov/sites/entrez/12406230 PubMed]
+
* '''Localization:'''
  
 
=== Database entries ===
 
=== Database entries ===
Line 84: Line 84:
 
* '''Swiss prot entry:'''
 
* '''Swiss prot entry:'''
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU15770]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU15760]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''
Line 94: Line 94:
 
* '''Operon:'''  
 
* '''Operon:'''  
  
−
* '''Sigma factor:'''  
+
* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
Line 122: Line 122:
 
=References=
 
=References=
  
−
# Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model  bacterium ''Bacillus subtilis''. Mol. Cell. Proteomics 6: 697-707  [http://www.ncbi.nlm.nih.gov/pubmed/17218307 PubMed]
+
# Obuchowski, M., Madec, E., Delattre, D., Boël, G., Iwanicki, A., Foulger, D. and Séror, S. J. 2000. Characterization of PrpC from ''Bacillus subtilis'', a member of the PPM phosphatase family. J. Bacteriol. 182: 5634-5638. [http://www.ncbi.nlm.nih.gov/sites/entrez/10986276 PubMed]
 
# Gaidenko TA, Kim TJ, Price CW: (2002) The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J Bacteriol, 184:6109-6114. [http://www.ncbi.nlm.nih.gov/sites/entrez/12399479 PubMed]
 
# Gaidenko TA, Kim TJ, Price CW: (2002) The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J Bacteriol, 184:6109-6114. [http://www.ncbi.nlm.nih.gov/sites/entrez/12399479 PubMed]
−
# Madec E, Laszkiewicz A, Iwanicki A, Obuchowski M, Séror S: (2002) Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes. Mol Microbiol, 46:571-586. [http://www.ncbi.nlm.nih.gov/sites/entrez/12406230 PubMed]
+
# Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537  PubMed]
−
# Madec E, Stensballe A, Kjellström S, Cladière L, Obuchowski M, Jensen ON, Séror S: (2003) 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 330:459-472. [http://www.ncbi.nlm.nih.gov/sites/entrez/12842463 PubMed]
 
−
# Shah IM, Laaberki MH, Popham DL, Dworkin J: A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 2008, 135:486-496. [http://www.ncbi.nlm.nih.gov/sites/entrez/18984160 PubMed]
 
 
# Absalon C, Obuchowski M, Madec E, Delattre D, Holland IB, Séror SJ (2009) CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in ''Bacillus subtilis''. ''Microbiology'' '''155:''' 932-943. [http://www.ncbi.nlm.nih.gov/sites/entrez/19246764 PubMed]
 
# Absalon C, Obuchowski M, Madec E, Delattre D, Holland IB, Séror SJ (2009) CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in ''Bacillus subtilis''. ''Microbiology'' '''155:''' 932-943. [http://www.ncbi.nlm.nih.gov/sites/entrez/19246764 PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 19:53, 15 April 2009

  • Description: protein phosphatase

Gene name prpC
Synonyms yloO
Essential no
Product protein phosphatase
Function antagonist of PrkC-dependent phosphorylation
MW, pI 27 kDa, 4.355
Gene length, protein length 762 bp, 254 aa
Immediate neighbours yloN, prkC
Hier soll was neues rein
Genetic context
PrpC context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Proteins dephosphorylated by PrpC

CpgA, EF-Tu, YezB PubMed, HPr PubMed

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

  1. Obuchowski, M., Madec, E., Delattre, D., Boël, G., Iwanicki, A., Foulger, D. and Séror, S. J. 2000. Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family. J. Bacteriol. 182: 5634-5638. PubMed
  2. Gaidenko TA, Kim TJ, Price CW: (2002) The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J Bacteriol, 184:6109-6114. PubMed
  3. Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. PubMed
  4. Absalon C, Obuchowski M, Madec E, Delattre D, Holland IB, Séror SJ (2009) CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology 155: 932-943. PubMed
  5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
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