Difference between revisions of "YosS"

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=References=
 
=References=
<pubmed>21358047 19342774 22383849</pubmed>
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<pubmed>21358047 19342774 22383849 23897460 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:46, 30 August 2013

  • Description: dUTP diphosphatase

Gene name yosS
Synonyms
Essential no
Product dUTP diphosphatase
Function nucleotide metabolism
Gene expression levels in SubtiExpress: yosS
MW, pI 16 kDa, 7.086
Gene length, protein length 426 bp, 142 aa
Immediate neighbours yosT, yosR
Sequences Protein DNA DNA_with_flanks
Genetic context
YosS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YosS expression.png















Categories containing this gene/protein

nucleotide metabolism/ other, SP-beta prophage

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU20020

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): YncF

Extended information on the protein

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

Database entries

  • 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

Javier García-Nafría, Jennifer Timm, Charlotte Harrison, Johan P Turkenburg, Keith S Wilson
Tying down the arm in Bacillus dUTPase: structure and mechanism.
Acta Crystallogr D Biol Crystallogr: 2013, 69(Pt 8);1367-80
[PubMed:23897460] [WorldCat.org] [DOI] (I p)

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)

Javier García-Nafría, Maria Harkiolaki, Rebecca Persson, Mark J Fogg, Keith S Wilson
The structure of Bacillus subtilis SPβ prophage dUTPase and its complexes with two nucleotides.
Acta Crystallogr D Biol Crystallogr: 2011, 67(Pt 3);167-75
[PubMed:21358047] [WorldCat.org] [DOI] (I p)

Gui Lan Li, Juan Wang, Lan Fen Li, Xiao Dong Su
Crystallization and preliminary X-ray analysis of three dUTPases from Gram-positive bacteria.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2009, 65(Pt 4);339-42
[PubMed:19342774] [WorldCat.org] [DOI] (I p)