Difference between revisions of "FtsZ"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 
+
* essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed], but dispensible in [[L-forms]] {{PubMed|25358088}}
essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 11:36, 31 October 2014

  • 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

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


Other original Publications