Acyltransferase; 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. Monomer. Impairs the production of emerecellamide A, C, D, E and F (PubMed:18559263). Belongs to the plant acyltransferase family.