The first five modules of the NRPS are encoded by the dptA gene and catalyze the condensation of L-tryptophan, D-aspartate, L-aspartate, L-threonine, and glycine, respectively (Figure 4). Modules 6-11, which catalyze the condensation of L-ornithine, L-aspartate, D-alanine, L-aspartate, glycine, and D-serine are encoded for the dptBC gene (Figure 5). DptD catalyzes the incorporation of two non-proteinogenic amino acids, L-3-methylglutamic acid (mGlu) and the unusual amino acid L-kynurenine (Kyn), which is only known thus far to Daptomycin, into the growing peptide (Figure 6). Elongation by these NRPS modules ultimately leads to macrocyclization and release in which an α-amino group, namely threonine, acts as an internal nucleophile during cyclization to yield the 10 amino acid ring (Figure 6). The termination module in the NRPS assembly line has a C-A-T-TE organization. The thioesterase (TE) domain catalyzes chain termination and release of the mature lipopeptide.