We have identified a gene involved in bacterial cell division, located immediately upstream of the
ftsI
gene in the min 2 region of the
Escherichia coli
chromosome. This gene, which we named
ftsL
, was detected through characterization of Tn
phoA
insertions in a plasmid containing this chromosomal region. Tn
phoA
topological analysis and fractionation of alkaline phosphatase fusion proteins indicated that the
ftsL
gene product is a 13.6-kDa cytoplasmic membrane protein with a cytoplasmic amino terminus, a single membrane-spanning segment, and a periplasmic carboxy terminus. The
ftsL
gene is essential for cell growth and division. A null mutation in
ftsL
resulted in inhibition of cell division, formation of long, nonseptate filaments, ultimate cessation of growth, and lysis. Under certain growth conditions, depletion of FtsL or expression of the largest
ftsL-phoA
fusion produced a variety of cell morphologies, including Y-shaped bacteria, indicating a possible general weakening of the cell wall. The FtsL protein is estimated to be present at about 20 to 40 copies per cell. The periplasmic domain of the protein displays a sequence with features characteristic of leucine zippers, which are involved in protein dimerization.