YaaO

• Description: similar to arginine decarboxylase, but without enzymatic activity
  
  

Gene name	yaaO
Synonyms
Essential	no
Product	putative arginine decarboxylase
Function	unknown
Gene expression levels in SubtiExpress: yaaO
Metabolic function and regulation of this protein in SubtiPathways: yaaO
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

sporulation proteins, poorly characterized/ putative enzymes

This gene is a member of the following regulons

SigW regulon, SigK regulon

The gene

Basic information

• Locus tag: BSU00270

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

Additional information

• the protein was reported to be involved in norspermidine production and biofilm disassembly PubMed; however, this is not the case PubMed

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • the protein was reported to be involved in norspermidine production and biofilm disassembly PubMed; however, this is not the case 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:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• UniProt: P37536

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: xpaC-yaaN-yaaO PubMed

• Expression browser: yaaO PubMed

• Sigma factor: SigW PubMed, SigK PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)