| Type: | Family | Name: | ATP binding protein MinD, bacterial-type |
| Description: | This entry describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. In Escherichia coli, the cell division site is determined by the cooperative activity of min operon products MinC, MinD, and MinE []. MinD is a membrane-associated ATPase and is a septum site-determining factor through the activation and regulation of MinC and MinE. MinD is also known to undergo a rapid pole-to-pole oscillation movement in vivo as observed by fluorescent microscopy. In plants, chloroplast division requires the dimerisation of stromal MinD []. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate entry. | Short Name: | MinD_bac-type |
