Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of emericellamides, secondary metabolites acting as antibiotics (PubMed:18559263). The biosynthesis of emericellamides initiates from the highly reducing polyketide synthase easB which catalyzes the formation of the linear polyketide chain (PubMed:18559263). EasB produces several polyketides that can be further processed by the downstream enzymes (PubMed:18559263). The polyketides are released from easB as linear polyketide carboxylic acids, which are converted to CoA thioesters by the acyl-CoA ligase easD (PubMed:18559263). The substrates are then loaded onto the acyltransferase easC, which shuttles them to the first thiolation (T) domain of the nonribosomal peptide synthetase easA (PubMed:18559263). EasA then performs condensation of the polyketides with one glycine, two alanine, one valine and one leucine residues (PubMed:18559263). A last step of cyclization leads to the production of emericellamides (PubMed:18559263). Antibiotic biosynthesis. The NRPS easA is a multimodular enzymatic assembly that contains 18 domains grouped into five modules corresponding to each of the five amino acid monomers incorporated (PubMed:18559263). The second to the fifth modules contain the three core domains, the condensation (C) domain responsible for catalyzing peptide bond formation, adenylation (A) domain responsible for selecting the amino acid monomer substrate, and the thiolation (T) domain (PubMed:18559263). The first module in the NRPS contains a unique T-E-C-A-T-E structure where (E) domains are epimerization domains (PubMed:18559263). The NRPS does not contain a TE domain at the end of module 5, presumably suggesting that TE is not necessary for the cyclization of the emericellamides (PubMed:18559263). Impairs the production of emerecellamide A, C, D, E and F (PubMed:18559263).