Difference between revisions of "EzrA"

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=== Basic information ===
 
=== Basic information ===
  
* '''Locus tag:'''
+
* '''Locus tag:''' BSU29610
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34894 O34894]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34894 O34894]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU29610 BSU29610]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU29610]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''

Revision as of 13:45, 3 June 2009

  • Description: negative regulator of FtsZ ring formation

Gene name ezrA
Synonyms ytwP
Essential no
Product FtsZ-interacting protein
Function control of FtsZ ring formation
MW, pI 64 kDa, 4.757
Gene length, protein length 1686 bp, 562 aa
Immediate neighbours braB, hisJ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
EzrA context.gif
This image was kindly provided by SubtiList




The gene

Basic information

  • Locus tag: BSU29610

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ezrA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cell membrane (according to Swiss-Prot), membrane associated PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • 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

Pamela Gamba, Jan-Willem Veening, Nigel J Saunders, Leendert W Hamoen, Richard A Daniel
Two-step assembly dynamics of the Bacillus subtilis divisome.
J Bacteriol: 2009, 191(13);4186-94
[PubMed:19429628] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)


  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed