Dynamin-related GTPase probably involved in membrane remodeling. Lipid and nucleotide-binding are thought to induce a large intramolecular rearrangement, leading to assembly on lipid bilayers and possible membrane curving. In the presence of the non-hydrolyzable GTP analog GMP-PNP self-assembles on a lipid bilayer; this does not stimulate subsequent GTPase activity. Does not bind lipids in the presence of GDP; perhaps GTP hydrolysis disrupts membrane-binding. GTP + H2O = GDP + H(+) + phosphate kcat is 0.53 min(-1). Homodimer. Self-assembles in the presence of GMP-PNP and liposomes, and probably also in the presence of GTP. Probably inserts into the outer leaflet of the membrane only (Probable). Forms foci localized in the cell periphery, and occasionally in the cell interior. Detected in vegetatively growing cells (at protein level). The GTPase domain dimerizes and forms the BDLP tube surface, the middle and GED domains are elongated and involved in self-assembly, while the paddle region inserts into the outer leaflet of the membrane, possibly promoting membrane curvature. Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.