Difference between revisions of "Sandbox"

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−
* '''Description:''' activity stimulated by ribosomes <br/><br/>
+
* '''Description:''' protein kinase C <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'''
−
|''cpgA ''
+
|''prkC''
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yloQ''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yloP ''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Product''' || GTPase
+
|style="background:#ABCDEF;" align="center"| '''Product''' || protein kinase
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown
+
|style="background:#ABCDEF;" align="center"|'''Function''' || germination in response to muropeptides
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 33 kDa, 4.743  
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 71 kDa, 4.833  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 894 bp, 298 aa  
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1944 bp, 648 aa  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[prkC]]'', ''[[rpe]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[prpC]]'', ''[[cpgA]]''
 
|-
 
|-
 
|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:yloQ_context.gif]]
+
|colspan="2" | '''Genetic context''' <br/> [[Image:prkC_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+BG13392]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG13391]
  
 
=== Additional information===
 
=== Additional information===
Line 57: Line 57:
  
 
* '''Paralogous protein(s):'''
 
* '''Paralogous protein(s):'''
 +
 +
=== 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]
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
Line 64: Line 68:
 
* '''Domains:'''  
 
* '''Domains:'''  
  
−
* '''Modification:''' phosphorylated on Ser/ Thr by [[PrkC]], dephosphorylated by [[PrpC]]  [http://www.ncbi.nlm.nih.gov/sites/entrez/19246764 PubMed]
+
* '''Modification:''' phosphorylation on Thr-290 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
−
* '''Effectors of protein activity:'''
+
* '''Effectors of protein activity:''' activated by muropeptides [http://www.ncbi.nlm.nih.gov/sites/entrez/18984160 PubMed]
  
 
* '''Interactions:'''
 
* '''Interactions:'''
  
−
* '''Localization:'''
+
* '''Localization:''' membrane [http://www.ncbi.nlm.nih.gov/sites/entrez/12406230 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===
Line 80: Line 84:
 
* '''Swiss prot entry:'''
 
* '''Swiss prot entry:'''
  
−
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU15780]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU15770]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''
Line 90: Line 94:
 
* '''Operon:'''  
 
* '''Operon:'''  
  
−
* '''[[Sigma factor]]:'''  
+
* '''Sigma factor:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
Line 113: Line 117:
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
−
 
−
[[Tony Wilkinson]], York University, U.K. [http://www.york.ac.uk/depts/chem/staff/ajw.html homepage]
 
  
 
=Your additional remarks=
 
=Your additional remarks=
Line 120: Line 122:
 
=References=
 
=References=
  
−
# Hunt, A., Rawlins, J. P., Thomaides, H. B., and Errington, J. (2006) Functional analysis of 11 putative essential genes in Bacillus subtilis. Microbiology 152, 2895-2907. [http://www.ncbi.nlm.nih.gov/sites/entrez/17005971 PubMed]
+
# 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]
 +
# 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]
 +
# 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]
−
# Absalon C, Hamze K, Blanot D, Frehel C, Carballido-Lopez R, Holland BI, van Heijenoort J, Séror SJ. (2008) The GTPase CpgA is implicated in the deposition of the peptidoglycan sacculus in Bacillus subtilis.  ''J Bacteriol.'' '''May;190(10):''' 3786-90. [http://www.ncbi.nlm.nih.gov/sites/entrez/18344364 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 kinase C

Gene name prkC
Synonyms yloP
Essential no
Product protein kinase
Function germination in response to muropeptides
MW, pI 71 kDa, 4.833
Gene length, protein length 1944 bp, 648 aa
Immediate neighbours prpC, cpgA
Hier soll was neues rein
Genetic context
PrkC 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 phosphorylated by PrkC

CpgA, EF-Tu, YezB PubMed, EF-G PubMed

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Thr-290 PubMed
  • Cofactor(s):
  • Effectors of protein activity: activated by muropeptides PubMed
  • Interactions:
  • Localization: membrane PubMed

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 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. 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. PubMed
  4. 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. PubMed
  5. 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. PubMed
  6. 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
  7. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
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