FtsZ

• 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
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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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
  • 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

• Interactions:
  • FtsZ-ZapA PubMed
  • FtsZ-EzrA PubMed
  • FtsZ-SpoIIE
  • FtsZ-FtsA
  • FtsZ-FtsZ PubMed
  • MciZ-FtsZ PubMed
  • FtsZ-SepF 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

Database entries

• Structure: 2VAM, 2RHL (dimer with GDP)

• UniProt: P17865

• 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

• Operon: ftsA-ftsZ PubMed

• Expression browser: ftsZ PubMed

• Sigma factor: SigA PubMed, SigH PubMed

• Regulation:
  • activated by WalR PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody: available in the Jeff Errington lab

Labs working on this gene/protein

• Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage
• Leendert Hamoen, CBCB, Newcastle University, UK

References

Reviews

Additional reviews: PubMed

An-Chun Chien, Norbert S Hill, Petra Anne Levin
Cell size control in bacteria.
Curr Biol: 2012, 22(9);R340-9
[PubMed:22575476] [WorldCat.org] [DOI] (I p)

Christine Kaimer, Peter L Graumann
Players between the worlds: multifunctional DNA translocases.
Curr Opin Microbiol: 2011, 14(6);719-25
[PubMed:22047950] [WorldCat.org] [DOI] (I p)

Clare L Kirkpatrick, Patrick H Viollier
New(s) to the (Z-)ring.
Curr Opin Microbiol: 2011, 14(6);691-7
[PubMed:21981908] [WorldCat.org] [DOI] (I p)

Matthew T Cabeen, Christine Jacobs-Wagner
The bacterial cytoskeleton.
Annu Rev Genet: 2010, 44;365-92
[PubMed:21047262] [WorldCat.org] [DOI] (I p)

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)

Peter L Graumann
Cytoskeletal elements in bacteria.
Annu Rev Microbiol: 2007, 61;589-618
[PubMed:17506674] [WorldCat.org] [DOI] (P p)

Linda A Amos, Fusinita van den Ent, Jan Löwe
Structural/functional homology between the bacterial and eukaryotic cytoskeletons.
Curr Opin Cell Biol: 2004, 16(1);24-31
[PubMed:15037301] [WorldCat.org] [DOI] (P p)

FtsZ as antibacterial drug target

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

Additional publications: PubMed