Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of sansalvamide, a cyclic pentadepsipeptide that shows promising results as potential anti-cancer drug (PubMed:26936154). The nonribosmal peptide synthetase NRPS30 produces sansalvamide by incorporating successively one phenylalanine, one leucine, one alpha-hydroxyisocaproic acid (HICA), one valine and one leucine before sansalvamide is released from by cyclization by the terminal C domain of NRPS30 (PubMed:26936154). The HICA residue is probably provided by reduction of alpha-ketoisocaproate by the cluster-specific aldo-keto reductase (NECHADRAFT_45914) (Probable). Secondary metabolite biosynthesis. NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase. NRPS30 has the following pentamodular architecture: A1-T1-C1-A2-T2-C2-A3-T3-C3-A4-T4-C4-A5-T5-C5. Abolishes the production of sansalvamide. Belongs to the NRP synthetase family.