Activates the second to fourth amino acids in tyrocidine (in tyrocidine A, Pro, Phe, and D-Phe) and epimerizes the last one. ATP + H2O + L-phenylalanine = AMP + D-phenylalanine + diphosphate + H(+) Binds 3 phosphopantetheines covalently. Antibiotic biosynthesis; tyrocidine biosynthesis. Large multienzyme complex of TycA, TycB and TycC. Consists of three modules, including a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional), and N methylation (optional). Tyrocidine is a mixture of four cyclic decapeptides, tyrocidine A (D-Phe-Pro-Phe-D-Phe-Asn-Gln-Tyr-Val-Orn-Leu), B, C, and D, in which Phe, at positions 3, 4, and Tyr residues are gradually replaced by Trp, depending on the relative concentrations of these amino acids in the growth medium. Belongs to the ATP-dependent AMP-binding enzyme family.