Difference between revisions of "ZapA"

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* '''Description:''' positive modulator of Z ring assembly and stability <br/><br/>
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* '''Description:''' positive modulator of [[FtsZ]] Z ring assembly and stability <br/><br/>
  
 
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{| align="right" border="1" cellpadding="2"  
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' forms a dimer through its extensive coiled-coil region
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* '''Interactions:''' forms a dimer through its extensive coiled-coil region, [[FtsZ]]-[[ZapA]] {{PubMed|19843223}}
  
 
* '''Localization:''' cell membrane (according to Swiss-Prot)
 
* '''Localization:''' cell membrane (according to Swiss-Prot)
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==Original Publications==
 
==Original Publications==
<pubmed>15288790,12368265,,18588879, 19429628 </pubmed>
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<pubmed>15288790,12368265,,18588879, 19429628 19843223 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:12, 22 October 2009

  • 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
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
YshA context.gif
This image was kindly provided by SubtiList



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:
  • Interactions: forms a dimer through its extensive coiled-coil region, FtsZ-ZapA PubMed
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [2]
  • 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

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

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)