Difference between revisions of "YaaO"

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m (Reverted edits by 134.76.70.252 (talk) to last revision by Jstuelk)
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yaaO_37720_39162_1 yaaO] {{PubMed|22383849}}
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=Biological materials =
 
=Biological materials =

Revision as of 10:46, 12 April 2012

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

Gene name yaaO
Synonyms
Essential no
Product putative arginine decarboxylase
Function unknown
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
YaaO context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

poorly characterized/ putative enzymes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU00270

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: 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

  • Operon:
  • Sigma factor:
  • 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

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)