Nonribosomal peptide synthesis (NRPS) is a key mechanism responsible for the biosynthesis of bioactive metabolites which are potentially contributing to organismal virulence. 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. NRPS7 has the following architecture: A-T-C-A-T-C. Belongs to the NRP synthetase family.