Only the N-terminal domain of FtsK functions in cell division.
Deletion of ftsK results in the inhibition of cell division, but this inhibition can be reversed by a plasmid carrying only the first approximately 17% of ftsK. The division block can be suppressed in most mutants by deletion of dacA, which codes for the D-alanine:D-alanine carboxypeptidase PBP5, or in all mutants by overexpression of ftsN. Overexpression of ftsK inhibits cell division and the formation of FtsZ rings. This division block is not due to the induction of either the SOS or the heat shock regulons.
Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland.
G C
GC
Draper
N
N
McLennan
K
K
Begg
M
M
Masters
W D
WD
Donachie
D001426:Bacterial Proteins / Q000737:chemistry / Q000502:physiology*; D001483:Base Sequence; D002455:Cell Division / Q000502:physiology*; D017931:DNA Primers; D029968:Escherichia coli Proteins; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D009154:Mutation; D010957:Plasmids; D011401:Promoter Regions, Genetic; D013014:SOS Response, Genetics; D017384:Sequence Deletion
D001426:Bacterial Proteins; D017931:DNA Primers; D029968:Escherichia coli Proteins; C096452:FtsK protein, E coli; D008565:Membrane Proteins