Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of beauveriolides I and III, cyclodepsipeptides acting as inhibitors of the acyl-CoA:cholesterol acyltransferase (PubMed:31926180). The HR-PKS cm3B initiates the biosynthesis of beauveriolides by iteratively catalyzing the formation of the linear polyketide chain (Probable). The ATP-dependent acetyl-CoA ligase cm3D converts the polyketide carboxylic acid to a CoA thioester which id shuttled to the first T domain in the NRPS cm3A by the acetyltransferase cm3C (Probable). Cm3A contains 13 domains and assembles the polyketide chain, L-phenylalanine, L-alanine, and D-leucine (or D-allo-isoleucine) to form beauveriolide I (or beauveriolide III). The production of both beauveriolides I and III suggests the substrate adaptability of cm3B, using different amino acids as substrates (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. Cm3A has the following module architecture: T-C-A-T-C-C-A-T-C-A-T-C-C. Beauveriolides inhibit selectively the acyl-CoA:cholesterol acyl-transferases (ACATs), leading to blocking the synthesis of cholesteryl esters and decreasing the cholesterol concentration, which suggests that beauveriolides are promising as potential lead compounds for antiatherosclerotic agents (PubMed:14718664, PubMed:19336931). Moreover, this activity correlates with inhibitory activities of beauveriolides in the secretion of amyloid-beta-peptide, which suggests that beauveriolides may be an attractive new candidate for the treatment of Alzheimer's disease (PubMed:19396893). Belongs to the nrps family.