FtsZ

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  • 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
Gene expression levels in SubtiExpress: ftsZ
Interactions involving this protein in SubtInteract: FtsZ
MW, pI 40 kDa, 4.814
Gene length, protein length 1146 bp, 382 aa
Immediate neighbours ftsA, bpr
Sequences Protein DNA DNA_with_flanks
Genetic context
FtsZ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FtsZ expression.png















Categories containing this gene/protein

cell division, essential genes, membrane proteins

This gene is a member of the following regulons

SigH regulon, WalR regulon

The gene

Basic information

  • Locus tag: BSU15290

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

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:
    • Z ring formation is inhibited upon binding of MciZ to FtsZ
    • bundling of FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules requires the prior formation of large ring polymers of SepF PubMed
    • interaction with UgtP inhibits FtsZ filament formation PubMed
    • FtsZ polymerization is inhibited by interaction with MinC PubMed
    • Z ring formation requires PdhA in a pyruvate-dependent manner PubMed
  • Localization:
    • septal at the cell membrane PubMed
    • septal localization partially depends on the proton motive force PubMed
    • Noc and the Min system ensure the efficient utilization of the division site at midcell in by ensuring Z ring placement PubMed
    • FtsZ is anchored to the cell membrane by either FtsA or SepF PubMed

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

    • the novel antibiotic ADEP (acyldepsipeptides) causes FtsZ degradation via dysregulation ClpP activity (activity occurs even in the absence of an ATPase subunit (ClpC, ClpE, or ClpX)) PubMed

Expression and regulation

  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2347 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 4359 PubMed

Biological materials

  • Mutant:
  • strains:
    • GP1372 (Pxyl ftsZ aphA3) disA::tet cdaS::ermC for xylose inducible expression of ftsZ, available in Jörg Stülke's lab
  • Expression vector:
    • GP2009: expression of ftsZ-Strep under control of the ftsZ promoter (based on pGP1389), available in Jörg Stülke's lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

Labs working on this gene/protein

Your additional remarks

References

Reviews


FtsZ as antibacterial drug target

Ewa Król, Anabela de Sousa Borges, Isabel da Silva, Carlos R Polaquini, Luis O Regasini, Henrique Ferreira, Dirk-Jan Scheffers
Antibacterial activity of alkyl gallates is a combination of direct targeting of FtsZ and permeabilization of bacterial membranes.
Front Microbiol: 2015, 6;390
[PubMed:25972861] [WorldCat.org] [DOI] (P e)

Sridevi Duggirala, Rakesh P Nankar, Selvakumar Rajendran, Mukesh Doble
Phytochemicals as inhibitors of bacterial cell division protein FtsZ: coumarins are promising candidates.
Appl Biochem Biotechnol: 2014, 174(1);283-96
[PubMed:25062781] [WorldCat.org] [DOI] (I p)

Dipty Singh, Anusri Bhattacharya, Ankit Rai, Hemendra Pal Singh Dhaked, Divya Awasthi, Iwao Ojima, Dulal Panda
SB-RA-2001 inhibits bacterial proliferation by targeting FtsZ assembly.
Biochemistry: 2014, 53(18);2979-92
[PubMed:24749867] [WorldCat.org] [DOI] (I p)

Filipa Marcelo, Sonia Huecas, Laura B Ruiz-Ávila, F Javier Cañada, Almudena Perona, Ana Poveda, Sonsoles Martín-Santamaría, Antonio Morreale, Jesús Jiménez-Barbero, José M Andreu
Interactions of bacterial cell division protein FtsZ with C8-substituted guanine nucleotide inhibitors. A combined NMR, biochemical and molecular modeling perspective.
J Am Chem Soc: 2013, 135(44);16418-28
[PubMed:24079270] [WorldCat.org] [DOI] (I p)

Laura B Ruiz-Avila, Sonia Huecas, Marta Artola, Albert Vergoñós, Erney Ramírez-Aportela, Emilia Cercenado, Isabel Barasoain, Henar Vázquez-Villa, Mar Martín-Fontecha, Pablo Chacón, María L López-Rodríguez, José M Andreu
Synthetic inhibitors of bacterial cell division targeting the GTP-binding site of FtsZ.
ACS Chem Biol: 2013, 8(9);2072-83
[PubMed:23855511] [WorldCat.org] [DOI] (I p)

Anusri Bhattacharya, Bhavya Jindal, Parminder Singh, Anindya Datta, Dulal Panda
Plumbagin inhibits cytokinesis in Bacillus subtilis by inhibiting FtsZ assembly--a mechanistic study of its antibacterial activity.
FEBS J: 2013, 280(18);4585-99
[PubMed:23841620] [WorldCat.org] [DOI] (I p)

David W Adams, Ling Juan Wu, Lloyd G Czaplewski, Jeff Errington
Multiple effects of benzamide antibiotics on FtsZ function.
Mol Microbiol: 2011, 80(1);68-84
[PubMed:21276094] [WorldCat.org] [DOI] (I p)

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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