Difference between revisions of "Sandbox"

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* '''Description:''' acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase) <br/><br/>
+
* '''Description:''' acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase) <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'''
|''acoL''
+
|''acoC''
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yfjH ''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yfjI ''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase)
+
|style="background:#ABCDEF;" align="center"| '''Product''' || acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Function''' || acetoin utilization  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || acetoin utilization  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 48 kDa, 5.273  
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 42 kDa, 6.524  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1374 bp, 458 aa  
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1194 bp, 398 aa  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[acoC]]'', ''[[acoR]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[acoB]]'', ''[[acoL]]''
 
|-
 
|-
 
|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:acoL_context.gif]]
+
|colspan="2" | '''Genetic context''' <br/> [[Image:acoC_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:''' [http://dbtbs.hgc.jp/COG/prom/acoABCL.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/acoABCL.html]
  
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12561]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12560]
  
 
=== Additional information===
 
=== Additional information===
Line 72: Line 72:
 
* '''Interactions:'''
 
* '''Interactions:'''
  
* '''Localization:'''
+
* '''Localization:''' Membrane-proximal (Spotty) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===
Line 80: Line 80:
 
* '''Swiss prot entry:'''
 
* '''Swiss prot entry:'''
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU08090]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU08080]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''
Line 121: Line 121:
  
  
 +
# Meile et al. (2006) Systematic localisation of proteins fused to the green fluorescent protein in ''Bacillus subtilis'': identification of new proteins at the DNA replication factory ''Proteomics'' '''6:''' 2135-2146. [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
 
# Ali, N. O., Bignon, J., Rapoport, G., and Débarbouillé, M. (2001) Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis. J. Bacteriol. 183, 2497-2504. [http://www.ncbi.nlm.nih.gov/sites/entrez/11274109  PubMed]
 
# Ali, N. O., Bignon, J., Rapoport, G., and Débarbouillé, M. (2001) Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis. J. Bacteriol. 183, 2497-2504. [http://www.ncbi.nlm.nih.gov/sites/entrez/11274109  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 20:48, 15 April 2009

  • Description: acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)

Gene name acoC
Synonyms yfjI
Essential no
Product acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)
Function acetoin utilization
MW, pI 42 kDa, 6.524
Gene length, protein length 1194 bp, 398 aa
Immediate neighbours acoB, acoL
Hier soll was neues rein
Genetic context
AcoC context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: Membrane-proximal (Spotty) PubMed

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: repressed by glucose (CcpA) , induced by acetoin (AcoR) PubMed
  • Regulatory mechanism: CcpA: transcription repression, AcoR: transcription activation (interaction with SigL-containing RNA polymerase) PubMed
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Michel Debarbouille, Pasteur Institute, Paris, France Homepage

Your additional remarks

References

  1. Meile et al. (2006) Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory Proteomics 6: 2135-2146. PubMed
  2. Ali, N. O., Bignon, J., Rapoport, G., and Débarbouillé, M. (2001) Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis. J. Bacteriol. 183, 2497-2504. PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed