Difference between revisions of "YaaO"
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<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[miscellaneous metabolic pathways]]}}, | {{SubtiWiki category|[[miscellaneous metabolic pathways]]}}, | ||
| − | {{SubtiWiki category|[[biofilm formation]]}} | + | {{SubtiWiki category|[[biofilm formation]]}}, |
| + | {{SubtiWiki category|[[sporulation proteins]]}} | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| − | + | {{SubtiWiki regulon|[[SigW regulon]]}}, | |
| + | {{SubtiWiki regulon|[[SigK regulon]]}} | ||
=The gene= | =The gene= | ||
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=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''[[xpaC]]-[[yaaN]]-[[yaaO]]'' {{PubMed|22383849}} |
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yaaO_37720_39162_1 yaaO] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yaaO_37720_39162_1 yaaO] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' [[SigW]] [http://www.ncbi.nlm.nih.gov/sites/entrez/9987136 PubMed], [[SigK]] {{PubMed|22383849}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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=References= | =References= | ||
| − | <pubmed> 20876533 22541437 </pubmed> | + | <pubmed> 20876533 22541437 22383849 9987136</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:34, 8 May 2013
- Description: carboxynorspermidine decarboxylase
| Gene name | yaaO |
| Synonyms | |
| Essential | no |
| Product | carboxynorspermidine decarboxylase |
| Function | synthesis of norspermidine |
| Gene expression levels in SubtiExpress: yaaO | |
| Metabolic function and regulation of this protein in SubtiPathways: Nucleotides (regulation) | |
| MW, pI | 52 kDa, 5.713 |
| Gene length, protein length | 1440 bp, 480 aa |
| Immediate neighbours | yaaN, tmk |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
miscellaneous metabolic pathways, biofilm formation, sporulation proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU00270
Phenotypes of a mutant
- impaired biofilm disassembly PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- catalyzes the last step in norspermidine synthesis PubMed
- Protein family: Orn/Lys/Arg decarboxylase class-I family (according to Swiss-Prot)
- Paralogous protein(s): SpeA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P37536
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- 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
Ilana Kolodkin-Gal, Shugeng Cao, Liraz Chai, Thomas Böttcher, Roberto Kolter, Jon Clardy, Richard Losick
A self-produced trigger for biofilm disassembly that targets exopolysaccharide.
Cell: 2012, 149(3);684-92
[PubMed:22541437]
[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)
Matthew Burrell, Colin C Hanfrey, Ewan J Murray, Nicola R Stanley-Wall, Anthony J Michael
Evolution and multiplicity of arginine decarboxylases in polyamine biosynthesis and essential role in Bacillus subtilis biofilm formation.
J Biol Chem: 2010, 285(50);39224-38
[PubMed:20876533]
[WorldCat.org]
[DOI]
(I p)
X Huang, A Gaballa, M Cao, J D Helmann
Identification of target promoters for the Bacillus subtilis extracytoplasmic function sigma factor, sigma W.
Mol Microbiol: 1999, 31(1);361-71
[PubMed:9987136]
[WorldCat.org]
[DOI]
(P p)
