Figure 1

Lipoprotein biogenesis in Streptomyces coelicolor.
Approximately 80% of precursor lipoproteins in S. coelicolor are translocated via the general secretory (Sec) pathway with around 20% being translocated by the twin arginine transport (Tat) pathway (a). Following translocation across the cytoplasmic membrane they are diacylated on the thiol of the lipobox (+1) cysteine residue by Lgt1 or Lgt (b) and then the signal sequence is cleaved by Lsp immediately upstream of that modified cysteine (c). Lnt1 then adds a third acyl chain to the amino group on the +1 cysteine to produce a triacylated lipoprotein (d). Lnt2 is not essential for triacylation in vitro but appears to increase its efficiency. The function of the N-acyl modification is not yet known.