|PROSITE documentation PDOC00873 [for PROSITE entry PS01135]|
In bacteria, ftsZ [1,2] is an essential cell division protein involved in cytokinesis. It assembles into a ring on the inner surface of the cytoplasmic membrane at the place where division will occur. The ring serves as a scaffold that is disassembled when septation is completed. FtsZ is a GTP binding protein with a GTPase activity. It undergoes GTP-dependent polymerization into filaments (or tubules) that seem to form a cytoskeleton involved in septum synthesis.
FtsZ is a protein of about 400 residues which is well conserved across bacterial species and which is also present in the chloroplast of plants  as well as in archaebacteria . FtsZ shows a limited similarity with eukaryotic tubulins. This similarity is probably both evolutionary and functionally significant.
As signature patterns we selected two glycine-rich conserved regions. The second region is equivalent to the GTP-binding region of tubulins (see <PDOC00199>).Last update:
December 2004 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|Title||FtsZ ring in bacterial cytokinesis.|
|Source||Mol. Microbiol. 9:403-409(1993).|
|Title||FtsZ, a prokaryotic homolog of tubulin?|
|3||Authors||Osteryoung K.W., Vierling E.|
|Title||Conserved cell and organelle division.|
|4||Authors||Margolin W., Wang R., Kumar M.|
|Title||Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin.|
|Source||J. Bacteriol. 178:1320-1327(1996).|