InterPro domain: IPR025501

MinD is 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 [ 1 ]. 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 [ 2 ]. Homologues can also be found in archaea, their exact role unknown.

FleN is involved in the maintenance of flagellar number in Pseudomonas aeruginosa 3 . It has been shown to be an anti-activator against FleQ, an important transcriptional regulator of flagellar genes 4 .

This entry represents an ATPase that includes both a MinD-type, and FleN-type.

1. The three-dimensional structure of septum site-determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP. Structure 9, 817-26
2. Chloroplast division site placement requires dimerization of the ARC11/AtMinD1 protein in Arabidopsis. J. Cell. Sci. 117, 2399-410
3. fleN, a gene that regulates flagellar number in Pseudomonas aeruginosa. J. Bacteriol. 182, 357-64
4. The FleQ protein from Pseudomonas aeruginosa functions as both a repressor and an activator to control gene expression from the pel operon promoter in response to c-di-GMP. Nucleic Acids Res. 40, 7207-18