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PROSITE documentation PDOC00873 [for PROSITE entry PS01134]

FtsZ protein signatures


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 [3] as well as in archaebacteria [4]. 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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

FTSZ_1, PS01134; FtsZ protein signature 1  (PATTERN)

FTSZ_2, PS01135; FtsZ protein signature 2  (PATTERN)


1AuthorsLutkenhaus J.
TitleFtsZ ring in bacterial cytokinesis.
SourceMol. Microbiol. 9:403-409(1993).
PubMed ID8412689

2AuthorsErickson H.P.
TitleFtsZ, a prokaryotic homolog of tubulin?
SourceCell 80:367-370(1995).
PubMed ID7859278

3AuthorsOsteryoung K.W., Vierling E.
TitleConserved cell and organelle division.
SourceNature 376:473-474(1995).
PubMed ID7637778

4AuthorsMargolin W., Wang R., Kumar M.
TitleIsolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin.
SourceJ. Bacteriol. 178:1320-1327(1996).
PubMed ID8631708

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