PROSITE logo
Black ribbon
We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00873
FtsZ protein signatures


View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00873

Description

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)


References

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
DOI10.1038/376473b0

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



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.