Difference between revisions of "EzrA"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
+ | ** degradation of [[EzrA]] involves [[FtsH]] {{PubMed|24222488}} | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** degradation of [[EzrA]] involves [[FtsH]] {{PubMed|24222488}} | ||
=Biological materials = | =Biological materials = | ||
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<pubmed> 19680248 19884039 </pubmed> | <pubmed> 19680248 19884039 </pubmed> | ||
==Original Publications== | ==Original Publications== | ||
− | <pubmed>10449747,16420366,15317782,16549676,17662947,12368265,18363795,9387221 15317798 , 19429628, 18763711 21401734 23701187</pubmed> | + | <pubmed>10449747,16420366,15317782,16549676,17662947,12368265,18363795,9387221 15317798 , 19429628, 18763711 21401734 24222488 23701187</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 12:50, 14 November 2013
- 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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
- 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):
- Localization: membrane associated PubMed
- 1 transmembrane domain at the N-terminus according to SOSUI
Database entries
- Structure:
- UniProt: O34894
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- constitutively expressed PubMed
- Regulatory mechanism:
Biological materials
- 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
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)
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)
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)