InterPro : IPR000158

Name  Cell division protein FtsZ Short Name  Cell_div_FtsZ
Type  Family Description  In bacteria, FtsZ [, , ]is an essential cell division protein which appears to be involved in the initiation of this event. It assembles into a cytokinetic 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 ring formation is initiated at a singlesite on one side of the bacterium and appears to grow bidirectionally. In Escherichia coli, MinCD , encoded by the MinB locus, form a complex which appears to block the formation of FtsZ rings at the cell poles, at the ancient mid cell division sites, whilst MinE, encoded at the same locus, specifically prevents the action of MinCD at mid cell.FtsZ is a GTP binding protein with a GTPase activity. It undergoes GTP-dependent polymerisation into filaments (or tubules) that seem to form a cytoskeleton involved in septum synthesis. The structure and the properties of FtsZ clearly provide it with the capacity for the cytoskeletal, perhaps motor role, necessary for "contraction" along the division plane. In addition, however, the FtsZ ring structure provides the framework for the recruitment or assembly of the ten or so membrane and cytoplasmic proteins, uniquely required for cell division in E. coli or Bacillus subtilis, some of which are required for biogenesis of the new hemispherical poles of the two daughter cells. FtsZ can polymerise into various structures, for example a single linear polymer of FtsZ monomers, called a protofilament. Protofilaments can associate laterally to form pairs (sometimes called thick filaments), bundles (ill-defined linear associations of multiple protofilaments) or thick filaments, sheets (parallel or anti-parallel two-dimensional associations of thick filaments) and tubes (anti-parallel associations of thick filaments in a circular fashion to form a tubular structure). In addition, small circles of FtsZ monomers (a short protofilament bent around to join itself, apparently head to tail) have been observed and termed mini-rings. 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 structural similarity with eukaryotic tubulins. This similarity is probably both evolutionary andfunctionally significant.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

4 Contains

Id Name Short Name Type
IPR003008 Tubulin/FtsZ, GTPase domain Tubulin_FtsZ_GTPase Domain
IPR008280 Tubulin/FtsZ, C-terminal Tub_FtsZ_C Domain
IPR018316 Tubulin/FtsZ, 2-layer sandwich domain Tubulin/FtsZ_2-layer-sand-dom Domain
IPR020805 Cell division protein FtsZ, conserved site Cell_div_FtsZ_CS Conserved_site

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Erickson HP FtsZ, a prokaryotic homolog of tubulin? 1995 Cell 80 367-70
Margolin W Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin. 1996 J Bacteriol 178 1320-7
Lutkenhaus J FtsZ ring in bacterial cytokinesis. 1993 Mol Microbiol 9 403-9
Osteryoung KW Conserved cell and organelle division. 1995 Nature 376 473-4
Addinall SG The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis. 2002 J Mol Biol 318 219-36

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)