Nonribosomal peptide synthase; part of the siderophore biosynthetic pathway (PubMed:26960149). Arthroderma benhamiae produces 2 types of extracellular siderophores, ferrichrome C and ferricrocin (PubMed:26960149). The biosynthesis of these siderophores depends on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by the monooxygenase sidA (PubMed:26960149). The structure of ferricrocin differs from ferrichrome C only by a serine for alanine substitution and the assembly of both siderophores is suggested to be performed by the nonribosomal peptide synthase (NRPS) sidC (PubMed:26960149). Siderophore biosynthesis. Expression is under the control of the iron acquisition regulator hapX (PubMed:26960149). 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 (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). 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 (By similarity). Occasionally, methyltransferase domains (responsible for amino acid methylation) are present within the NRP synthetase (By similarity). SidC has the following architecture: A-T-C-A-T-C-T-C-A-T-C-T-C-T-C. Belongs to the NRP synthetase family.