Difference between revisions of "EzrA"

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=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:'''  
+
* '''Operon:''' ''[[ezrA]]'' {{PubMed|9387221}}
  
* '''[[Sigma factor]]:'''  
+
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|15317798}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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<pubmed> 19680248  19884039 </pubmed>
 
<pubmed> 19680248  19884039 </pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>10449747,16420366,15317782,16549676,17662947,12368265,18363795,, 19429628, 18763711 </pubmed>
+
<pubmed>10449747,16420366,15317782,16549676,17662947,12368265,18363795,9387221 15317798 , 19429628, 18763711 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:19, 19 December 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: membrane associated PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • 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

Reviews

Marc Bramkamp, Suey van Baarle
Division site selection in rod-shaped bacteria.
Curr Opin Microbiol: 2009, 12(6);683-8
[PubMed:19884039] [WorldCat.org] [DOI] (I p)

David W Adams, Jeff Errington
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
Nat Rev Microbiol: 2009, 7(9);642-53
[PubMed:19680248] [WorldCat.org] [DOI] (I p)

Original Publications

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)

Dennis Claessen, Robyn Emmins, Leendert W Hamoen, Richard A Daniel, Jeff Errington, David H Edwards
Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis.
Mol Microbiol: 2008, 68(4);1029-46
[PubMed:18363795] [WorldCat.org] [DOI] (I p)

Richard B Weart, Amy H Lee, An-Chun Chien, Daniel P Haeusser, Norbert S Hill, Petra Anne Levin
A metabolic sensor governing cell size in bacteria.
Cell: 2007, 130(2);335-47
[PubMed:17662947] [WorldCat.org] [DOI] (P p)

Yoshikazu Kawai, Naotake Ogasawara
Bacillus subtilis EzrA and FtsL synergistically regulate FtsZ ring dynamics during cell division.
Microbiology (Reading): 2006, 152(Pt 4);1129-1141
[PubMed:16549676] [WorldCat.org] [DOI] (P p)

Leendert W Hamoen, Jean-Christophe Meile, Wouter de Jong, Philippe Noirot, Jeff Errington
SepF, a novel FtsZ-interacting protein required for a late step in cell division.
Mol Microbiol: 2006, 59(3);989-99
[PubMed:16420366] [WorldCat.org] [DOI] (P p)

Kuei-Min Chung, Hsin-Hsien Hsu, Suresh Govindan, Ban-Yang Chang
Transcription regulation of ezrA and its effect on cell division of Bacillus subtilis.
J Bacteriol: 2004, 186(17);5926-32
[PubMed:15317798] [WorldCat.org] [DOI] (P p)

David E Anderson, Frederico J Gueiros-Filho, Harold P Erickson
Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.
J Bacteriol: 2004, 186(17);5775-81
[PubMed:15317782] [WorldCat.org] [DOI] (P p)

Frederico J Gueiros-Filho, Richard Losick
A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ.
Genes Dev: 2002, 16(19);2544-56
[PubMed:12368265] [WorldCat.org] [DOI] (P p)

P A Levin, I G Kurtser, A D Grossman
Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1999, 96(17);9642-7
[PubMed:10449747] [WorldCat.org] [DOI] (P p)

Alia Lapidus, Nathalie Galleron, Alexei Sorokin, S Dusko Ehrlich
Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.
Microbiology (Reading): 1997, 143 ( Pt 11);3431-3441
[PubMed:9387221] [WorldCat.org] [DOI] (P p)