Nonribosomal peptide synthetase that catalyzes the biosynthesis of the hydrophobic cyclopentapeptides malpibaldins, natural products that show biosurfactant activities (PubMed:33158886) (Probable). Module 3 shows promiscuous adenylation (accepting either Trp, Phe or Tyr) leading to the parallel production of multiple products from one NRPS assembly line, including malpibaldin A corresponding to cyclo(-L-Leu-D-Leu-D-Phe-L-Leu-D-Val-), malpibaldin B corresponding to cyclo(-L-Leu-D-Leu-D-Tyr-L-Leu-D-Val-) and malpibaldin C corresponding to cyclo(-Leu-Leu-Trp-Leu-Val-) (PubMed:33158886). Expression is induced in the presence of fructose. 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. Contains bacterial-like dual epimerase/condensation domains allowing the racemization of enzyme-tethered L-amino acids and the subsequent incorporation of D-amino acids into the metabolites. MpbA has the following architecture: C-A-T-E/C-A-T-C-A-T-E/C-A-T-E/C-A-T-TE. Mortierella alpina biosurfactants may have an enormous potential for various applications in pharmacy, health care, food, cosmetics, or textiles since they offer a highly biocompatible and biodegradable alternative for synthetic surfactants in formulations. The surprising structural and mechanistic similarity to bacterial nonribosomal peptide synthetases (NRPSs) points to an endobacterial origin of the Mortierella mpcA and mpbA genes that differ from their asco- and basidiomycete counterparts and may have evolved independently. Belongs to the NRP synthetase family.