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

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

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

• 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

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)

Additional reviews: PubMed

Other original Publications

Additional publications: PubMed