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
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 Advanced_DNA
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
  • interaction with UgtP inhibits FtsZ filament formation PubMed
  • FtsZ polymerization is inhibited by interaction with MinC PubMed

• Interactions:
  • FtsZ-ZapA PubMed
  • FtsZ-EzrA PubMed
  • FtsZ-SpoIIE
  • FtsZ-FtsA
  • FtsZ-FtsZ PubMed
  • MciZ-FtsZ PubMed
  • FtsZ (extreme C terminus of FtsZ)-SepF PubMed
  • RefZ-FtsZ PubMed
  • FtsZ-LytE PubMed
  • UgtP-FtsZ, this interaction inhibits FtsZ filament formation PubMed
  • FtsZ (C-terminal domain)-MinC 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

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)