Difference between revisions of "YjcK"

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(Biological materials)
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=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:'''  
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* '''Operon:''' ''[[yjcL]]-[[yjcK]]'' {{PubMed|22383849}}
  
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yjcK_1260811_1261356_-1 yjcK] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yjcK_1260811_1261356_-1 yjcK] {{PubMed|22383849}}
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** GP1246 (''yjcK''::''cat''), available in [[Jörg Stülke]]'s lab
 
** GP1246 (''yjcK''::''cat''), available in [[Jörg Stülke]]'s lab
 
** GP1255 (''[[acuA]]''::''kan'' ''[[yjcK]]''::''cat'' ''[[ynaD]]''::''spec'' ''[[yoaA]]''::''tet''), available in [[Jörg Stülke]]'s lab
 
** GP1255 (''[[acuA]]''::''kan'' ''[[yjcK]]''::''cat'' ''[[ynaD]]''::''spec'' ''[[yoaA]]''::''tet''), available in [[Jörg Stülke]]'s lab
** BP139 (''yjcKL''::''ermC''), available in [[Fabian Commichau]]'s lab
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** BP139 (''[[yjcL]]-[[yjcK]]''::''ermC''), available in [[Fabian Commichau]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
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=References=
 
=References=
  
<pubmed> 16479537 </pubmed>
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<pubmed> 16479537 22383849</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:20, 9 August 2013

  • Description: similar to ribosomal-protein-alanine N-acetyltransferase

Gene name yjcK
Synonyms
Essential no
Product unknown
Function unknown
Gene expression levels in SubtiExpress: yjcK
MW, pI 20 kDa, 5.459
Gene length, protein length 543 bp, 181 aa
Immediate neighbours metC, yjcL
Sequences Protein DNA DNA_with_flanks
Genetic context
YjcK context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YjcK expression.png















Categories containing this gene/protein

translation, protein modification

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU11890

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acetyl-CoA + ribosomal-protein L-alanine = CoA + ribosomal-protein N-acetyl-L-alanine (according to Swiss-Prot)
  • Protein family: N-acetyltransferase domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)