Difference between revisions of "YosS"
| Line 86: | Line 86: | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
| + | ** forms homotrimers {{PubMed|22383849}} | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
| Line 134: | Line 135: | ||
=References= | =References= | ||
| − | + | <pubmed>21358047 19342774 22383849</pubmed> | |
| − | <pubmed> 19342774 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 09:15, 31 July 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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
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:
- Interactions:
- forms homotrimers PubMed
Database entries
- UniProt: O34919
- 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
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)
