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ftsZ [2017-05-09 15:36:34]
cell-division initiation protein (septum formation)
Molecular weight
40.20 kDa
Function
formation of Z-ring
Product
cell-division initiation protein (septum formation)
Genomic Context
Categories containing this gene/protein
Gene
Coordinates
1,597,832 → 1,598,980
Phenotypes of a mutant
The protein
Protein family
ftsZ family (according to Swiss-Prot)Effectors of protein activity
Z ring formation is inhibited upon binding of F150B9B75C8352950B9BB71E29CB156B66AA6CDD to FtsZbundling of FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules requires the prior formation of large ring polymers of SepF PubMedinteraction with UgtP inhibits FtsZ filament formation PubMedFtsZ polymerization is inhibited by interaction with MinC PubMedZ ring formation requires PdhA in a pyruvate-dependent manner PubMed Structure
Localization
septal at the cell membrane PubMedseptal localization partially depends on the proton motive force PubMedNoc and the Min system ensure the efficient utilization of the division site at midcell in by ensuring Z ring]] placement PubMedFtsZ 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
Sigma factors
Regulatory mechanism
Regulation
Additional information
view in new tabBiological 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
Labs working on this gene/protein
References
Reviews
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FtsZ as antibacterial drug target
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Other original Publications
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