Difference between revisions of "ZapA"
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* '''Operon:''' ''[[zapA]]-[[yshB]]'' {{PubMed|12368265}} | * '''Operon:''' ''[[zapA]]-[[yshB]]'' {{PubMed|12368265}} | ||
− | * '''[ | + | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=yshA_2925640_2925897_-1 zapA] {{PubMed|22383849}} |
+ | |||
+ | * '''Sigma factor:''' | ||
* '''Regulation:''' | * '''Regulation:''' |
Revision as of 14:47, 16 April 2012
- Description: positive modulator of FtsZ Z ring assembly and stability
Gene name | zapA |
Synonyms | yshA |
Essential | no |
Product | Z-ring-associated protein |
Function | control of Z-ring formation |
Interactions involving this protein in SubtInteract: ZapA | |
MW, pI | 9 kDa, 7.17 |
Gene length, protein length | 255 bp, 85 aa |
Immediate neighbours | yshB, rnhC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
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: BSU28610
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: Type 2 subfamily (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)
Database entries
- Structure:
- UniProt: P94542
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- 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
Reviews
Original Publications
Leigh G Monahan, Andrew Robinson, Elizabeth J Harry
Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria.
Mol Microbiol: 2009, 74(4);1004-17
[PubMed:19843223]
[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)
Dirk-Jan Scheffers
The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA.
FEBS Lett: 2008, 582(17);2601-8
[PubMed:18588879]
[WorldCat.org]
[DOI]
(P p)
Harry H Low, Martin C Moncrieffe, Jan Löwe
The crystal structure of ZapA and its modulation of FtsZ polymerisation.
J Mol Biol: 2004, 341(3);839-52
[PubMed:15288790]
[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)