Difference between revisions of "YaaO"

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<pubmed> 20876533 22541437 22383849 9987136</pubmed>
<pubmed> 24529384 20876533 22541437 22383849 9987136</pubmed>
[[Category:Protein-coding genes]]
[[Category:Protein-coding genes]]

Revision as of 16:48, 25 February 2014

  • Description: carboxynorspermidine decarboxylase

Gene name yaaO
Essential no
Product carboxynorspermidine decarboxylase
Function synthesis of norspermidine
Gene expression levels in SubtiExpress: yaaO
Metabolic function and regulation of this protein in SubtiPathways:
MW, pI 52 kDa, 5.713
Gene length, protein length 1440 bp, 480 aa
Immediate neighbours yaaN, tmk
Sequences Protein DNA DNA_with_flanks
Genetic context
YaaO context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YaaO expression.png

Categories containing this gene/protein

miscellaneous metabolic pathways, biofilm formation, sporulation proteins

This gene is a member of the following regulons

SigW regulon, SigK regulon

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:
  • 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


Laura Hobley, Sok Ho Kim, Yukari Maezato, Susan Wyllie, Alan H Fairlamb, Nicola R Stanley-Wall, Anthony J Michael
Norspermidine is not a self-produced trigger for biofilm disassembly.
Cell: 2014, 156(4);844-54
[PubMed:24529384] [WorldCat.org] [DOI] (I p)

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)