Nonribosomal peptide synthetase; part of the gene cluster 14 that mediates the biosynthesis of a ferrichrome A-like siderophore which may contribute to organismal virulence (Probable). The first step of siderophore biosynthesis is performed by the HMG-CoA synthase (HMGS) MYCGRDRAFT_54740 which catalyzes the generation of HMG-CoA and CoA using acetoacetyl-CoA and acetyl-CoA as substrates (By similarity). The enoyl-CoA isomerase/hydratase MYCGRDRAFT_76805 then catalyzes the conversion of HMG-CoA to methylglutaconyl-CoA (By similarity). The acyltransferase MYCGRDRAFT_85486 then fuses methylglutaconyl-CoA with hydroxyornithine to yield methylglutaconyl hydroxyornithine (By similarity). Methylglutaconyl hydroxyornithine is then available for use by the nonribosomal peptide synthetase NRPS2 to generate the ferrichrome A-like siderophore (By similarity). Siderophore 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. NRPS2 has the following architecture: A-T-C-T-C-A-T-C-T-C-T-C (Probable). The lack of corresponding A domains in the 3 modules suggests that A domains have to be used iteratively to incorporate the six amino acids in the siderophore (By similarity). Belongs to the NRP synthetase family.