EzrA

From SubtiWiki
Revision as of 15:54, 10 April 2015 by Jstuelk (talk | contribs)
Jump to: navigation, search
  • Description: negative regulator of FtsZ ring formation

Gene name ezrA
Synonyms ytwP
Essential no
Product FtsZ-interacting protein
Function control of FtsZ ring formation
Gene expression levels in SubtiExpress: ezrA
Interactions involving this protein in SubtInteract: EzrA
MW, pI 64 kDa, 4.757
Gene length, protein length 1686 bp, 562 aa
Immediate neighbours braB, hisJ
Sequences Protein DNA DNA_with_flanks
Genetic context
EzrA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
EzrA expression.png















Categories containing this gene/protein

cell division, membrane proteins

This gene is a member of the following regulons

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

  • Protein family: ezrA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 4UXV (the 60 kDa cytoplasmic domain) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • constitutively expressed PubMed
  • Regulatory mechanism:
  • Additional information:
    • degradation of EzrA involves FtsH PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 125 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 495 PubMed

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

Frédérique Pompeo, Elodie Foulquier, Bastien Serrano, Christophe Grangeasse, Anne Galinier
Phosphorylation of the cell division protein GpsB regulates PrkC kinase activity through a negative feedback loop in Bacillus subtilis.
Mol Microbiol: 2015, 97(1);139-50
[PubMed:25845974] [WorldCat.org] [DOI] (I p)

Robert M Cleverley, Jeffrey R Barrett, Arnaud Baslé, Nhat Khai Bui, Lorraine Hewitt, Alexandra Solovyova, Zhi-Qiang Xu, Richard A Daniel, Nicholas E Dixon, Elizabeth J Harry, Aaron J Oakley, Waldemar Vollmer, Richard J Lewis
Structure and function of a spectrin-like regulator of bacterial cytokinesis.
Nat Commun: 2014, 5;5421
[PubMed:25403286] [WorldCat.org] [DOI] (I e)

Adrian D Land, Qingwei Luo, Petra Anne Levin
Functional domain analysis of the cell division inhibitor EzrA.
PLoS One: 2014, 9(7);e102616
[PubMed:25068683] [WorldCat.org] [DOI] (I e)

Leigh G Monahan, Isabella V Hajduk, Sinead P Blaber, Ian G Charles, Elizabeth J Harry
Coordinating bacterial cell division with nutrient availability: a role for glycolysis.
mBio: 2014, 5(3);e00935-14
[PubMed:24825009] [WorldCat.org] [DOI] (I e)

Benjamin Mielich-Süss, Johannes Schneider, Daniel Lopez
Overproduction of flotillin influences cell differentiation and shape in Bacillus subtilis.
mBio: 2013, 4(6);e00719-13
[PubMed:24222488] [WorldCat.org] [DOI] (I e)

Ramona Duman, Shu Ishikawa, Ilkay Celik, Henrik Strahl, Naotake Ogasawara, Paulina Troc, Jan Löwe, Leendert W Hamoen
Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring.
Proc Natl Acad Sci U S A: 2013, 110(48);E4601-10
[PubMed:24218584] [WorldCat.org] [DOI] (I p)

Katarina Surdova, Pamela Gamba, Dennis Claessen, Tjalling Siersma, Martijs J Jonker, Jeff Errington, Leendert W Hamoen
The conserved DNA-binding protein WhiA is involved in cell division in Bacillus subtilis.
J Bacteriol: 2013, 195(24);5450-60
[PubMed:24097947] [WorldCat.org] [DOI] (I p)

Erik Nico Trip, Jan-Willem Veening, Eric J Stewart, Jeff Errington, Dirk-Jan Scheffers
Balanced transcription of cell division genes in Bacillus subtilis as revealed by single cell analysis.
Environ Microbiol: 2013, 15(12);3196-209
[PubMed:23701187] [WorldCat.org] [DOI] (I p)

Victoria R Steele, Amy L Bottomley, Jorge Garcia-Lara, Jagath Kasturiarachchi, Simon J Foster
Multiple essential roles for EzrA in cell division of Staphylococcus aureus.
Mol Microbiol: 2011, 80(2);542-55
[PubMed:21401734] [WorldCat.org] [DOI] (I p)

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)

Jay Kumar Singh, Ravindra D Makde, Vinay Kumar, Dulal Panda
A membrane protein, EzrA, regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ.
Biochemistry: 2007, 46(38);11013-22
[PubMed:17718511] [WorldCat.org] [DOI] (P 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)

Retrieved from "http://subtiwiki-test.uni-goettingen.de/wiki//index.php?title=EzrA&oldid=207680"