The Mip-like protein of Chlamydia trachomatis is similar to the Mip pr
otein of Legionella pneumophila and may be equally important for the i
nitiation of intracellular infection. This article presents data which
identify the chlamydial Mip-like protein as a lipoprotein. The amino
acid sequence of the Mip-like protein contains a signal peptidase II r
ecognition sequence, as is seen in procaryotic lipoproteins. Palmitic
acid was incorporated into the recombinant chlamydial Mip-like protein
. Globomycin, known to inhibit signal peptidase II, inhibited processi
ng of the recombinant Mip-like protein. Labelling of chlamydial organi
sms with palmitic acid revealed incorporation into the native Mip-like
protein.