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ftsZ [2017-05-09 15:36:34]
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ftsZ [2017-05-09 15:36:34]

cell-division initiation protein (septum formation)
Locus
BSU15290
Isoelectric point
4.81
Molecular weight
40.20 kDa
Protein length
382 aa Sequence Blast
Gene length
1146 bp Sequence Blast
Function
formation of Z-ring
Product
cell-division initiation protein (septum formation)
Essential
yes
Synonyms
ts-1
Outlinks
KEGGBsubCycSubtiListUniProtExpression Browser

Genomic Context

      
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Categories containing this gene/protein

  • Cellular processes → Cell envelope and cell division → Cell division → Other genes
  • Groups of genes → Essential genes
  • Groups of genes → Membrane proteins

    • Gene

    Coordinates
    1,597,832 → 1,598,980

    Phenotypes of a mutant

  • essential PubMed, but dispensible in L-forms PubMed

    • The protein

    Protein family

  • ftsZ family (according to Swiss-Prot)

    • Effectors of protein activity

  • Z ring formation is inhibited upon binding of F150B9B75C8352950B9BB71E29CB156B66AA6CDD 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

    • Structure

  • 2VAM
  • 2RHL (dimer with GDP)
  • 4U39 (FtsZ-F150B9B75C8352950B9BB71E29CB156B66AA6CDD complex) 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

    • 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

    Operons

    Genes
    ftsA-ftsZ
    Description
    PubMed

    Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon
  • SigH: sigma factor, PubMed, in SigH regulon

    • Regulatory mechanism

  • WalR: activation, in WalR regulon

    • Regulation

  • activated by WalR PubMed

    • Additional information

  • half-life of the ftsZ mRNA: 2.2 min PubMed
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    Biological materials

    Expression vector

  • GP2009: expression of ftsZ-Strep under control of the ftsZ promoter (based on pGP1389), available in Jörg Stülke's lab

    • Two-hybrid system

  • B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

    • 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

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    FtsZ as antibacterial drug target

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    Other original Publications

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