Nonribisomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of valactamides (PubMed:28604695). The first step of the pathway is performed by the highly reducing polyketide synthase valA that produces the polyketide part of the final products (Probable). An acetyl starter unit is incorporated by the ketosynthase domain of valA, and subsequently 6 malonyl-CoA-derived ketide units are incorporated and fully reduced to their respective alkane forms by the action of the ketoreductase, dehydratase, and enoylreductase domains (except for the penultimate unit, which is reduced only to the alkene) (Probable). The final five ketide units are each proposed to be alpha-methylated by the methyltransferase domain before ketone reduction by the ketoreductase domain (Probable). The C1 domain of the nonribisomal peptide synthetase valB then catalyzes amide bond formation between the heptaketide chain and L-valine (L-Val) attached to the T1 domain (Probable). The C2 domain incorporating L-isoleucine (L-Ile) then carries out chain elongation, which is followed by macrolactonization by the Ct domain to release the final product (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. BenZ as the following bimodular architecture: C1-A1-T1-C2-A2-T2-Ct. Abolishes the production of valactamides A-H. Belongs to the NRP synthetase family.