Difference between revisions of "FtsZ"

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* '''Description:''' cell-division initiation protein (septum formation) <br/><br/>
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* '''Description:''' cell-division initiation protein (septum formation) &lt;br/>&lt;br/>
 
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ftsA]]'', ''[[bpr]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ftsA]]'', ''[[bpr]]''
 
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&amp;#91;EMBLCDS:CAB13402&amp;#93;+-newId sequences] &lt;br/> (Barbe ''et al.'', 2009)'''
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB13402&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
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|colspan="2" | '''Genetic context''' &lt;br/> [[Image:ftsZ_context.gif]]
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|colspan="2" | '''Genetic context''' <br/> [[Image:ftsZ_context.gif]]
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  &lt;div align="right"> &lt;small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]&lt;/small>&lt;/div>
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  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
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__TOC__
 
__TOC__
  
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<br/><br/>
  
 
=The gene=
 
=The gene=
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==Reviews==
 
==Reviews==
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&lt;pubmed> 19680248  19884039 17506674 15037301  &lt;/pubmed>
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<pubmed> 19680248  19884039 17506674 15037301  </pubmed>
  
 
==FtsZ as antibacterial drug target==
 
==FtsZ as antibacterial drug target==
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&lt;pubmed> 19583568 20410587 ,16174771, 20212044 20615583 &lt;/pubmed>
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<pubmed> 19583568 20410587 ,16174771, 20212044 20615583 </pubmed>
  
 
==Other original Publications==
 
==Other original Publications==
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&lt;pubmed> 15288790, 15317782,12180929, 9364910,10323866, 19212404,15942012, 12007411,16420366, 16159787,10747015, 16796675,10322023,9495766,9287012,1569582,10878122,11395470,10449747,17662947,12368265,18284588,8600030,18588879,7592498, 19136590 , 19429628, 19141479 19843223 16484179 20199598 20566861 20711458 20807205 20933427 &lt;/pubmed>
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<pubmed> 15288790, 15317782,12180929, 9364910,10323866, 19212404,15942012, 12007411,16420366, 16159787,10747015, 16796675,10322023,9495766,9287012,1569582,10878122,11395470,10449747,17662947,12368265,18284588,8600030,18588879,7592498, 19136590 , 19429628, 19141479 19843223 16484179 20199598 20566861 20711458 20807205 20933427 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 04:57, 24 November 2010

  • Description: cell-division initiation protein (septum formation)

Gene name ftsZ
Synonyms ts-1
Essential yes PubMed
Product cell-division initiation protein (septum formation)
Function formation of Z-ring
MW, pI 40 kDa, 4.814
Gene length, protein length 1146 bp, 382 aa
Immediate neighbours ftsA, bpr
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
FtsZ context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU15290

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ftsZ family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: Z ring formation is inhibited upon binding of MciZ to FtsZ
  • Localization:
    • septal at the cell membrane PubMed
    • septal localization partially depends on the proton motive force PubMed

Database entries

  • Structure: 2VAM, 2RHL (dimer with GDP)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage

Your additional remarks

References

Reviews


FtsZ as antibacterial drug target

Simranjeet Kaur, Niraj H Modi, Dulal Panda, Nilanjan Roy
Probing the binding site of curcumin in Escherichia coli and Bacillus subtilis FtsZ--a structural insight to unveil antibacterial activity of curcumin.
Eur J Med Chem: 2010, 45(9);4209-14
[PubMed:20615583] [WorldCat.org] [DOI] (I p)

Kumiko W Shimotohno, Fujio Kawamura, Yousuke Natori, Hideaki Nanamiya, Junji Magae, Hiromitsu Ogata, Toyoshige Endo, Takeshi Suzuki, Hiroshi Yamaki
Inhibition of septation in Bacillus subtilis by a peptide antibiotic, edeine B(1).
Biol Pharm Bull: 2010, 33(4);568-71
[PubMed:20410587] [WorldCat.org] [DOI] (I p)

José M Andreu, Claudia Schaffner-Barbero, Sonia Huecas, Dulce Alonso, María L Lopez-Rodriguez, Laura B Ruiz-Avila, Rafael Núñez-Ramírez, Oscar Llorca, Antonio J Martín-Galiano
The antibacterial cell division inhibitor PC190723 is an FtsZ polymer-stabilizing agent that induces filament assembly and condensation.
J Biol Chem: 2010, 285(19);14239-46
[PubMed:20212044] [WorldCat.org] [DOI] (I p)

Tushar K Beuria, Parminder Singh, Avadhesha Surolia, Dulal Panda
Promoting assembly and bundling of FtsZ as a strategy to inhibit bacterial cell division: a new approach for developing novel antibacterial drugs.
Biochem J: 2009, 423(1);61-9
[PubMed:19583568] [WorldCat.org] [DOI] (I e)

Neil R Stokes, Jörg Sievers, Stephanie Barker, James M Bennett, David R Brown, Ian Collins, Veronica M Errington, David Foulger, Michelle Hall, Rowena Halsey, Hazel Johnson, Valerie Rose, Helena B Thomaides, David J Haydon, Lloyd G Czaplewski, Jeff Errington
Novel inhibitors of bacterial cytokinesis identified by a cell-based antibiotic screening assay.
J Biol Chem: 2005, 280(48);39709-15
[PubMed:16174771] [WorldCat.org] [DOI] (P p)


Other original Publications

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