Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of KK-1, a novel cyclic decapeptide compound with potent antifungal activity (PubMed:29686660). The nonribosomal peptide synthetase (NRPS) catalyzes the elongation and cyclization of the decapeptide chain composed of 1 pipecolic acid residue (Pip), 1 alanine residue (Ala), 1 aspartic acid residue (Asp), 1 isoleucine residue (Ile), 1 glycine residue (Gly), 1 tyrosine residue (Tyr) and 4 valine residues (Val) (PubMed:29686660). The Asp, Ile and 3 Val residues are N-methylated by the 5 methyltransferase domains from the NRPS (found in modules 3, 5, 6, 7 and 9), whereas the Tyr residue is O-methylated, probably by the cluster encoded O-methyltransferase OMT (PubMed:29686660). The other tailoring enzymes from the cluster may be involved in further modifications leading to the synthesis of KK-1 (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, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetaseTES has the following 10 modules architecture: A1-T1-C1-A2-T2-C2-A3-M3-T3-C3-A4-T4-C4-A5-M5-T5-C5-A6-M6-T6-C6-A7-M7-T7-C7-A8-T8-C8-A9-M9-T9-C9-A10-T10-C10. Belongs to the NRP synthetase family.