The non-ribosomal peptide synthase (NRPS) is encoded by three genes: CepA, CepB, and CepC. CepA links the first three amino acids; CepB adds the fourth to sixth amino acids; CepC adds the last amino acid and includes a thioesterase domain to release the heptapeptide from the NRPS complex. The growing peptide chain is passed through modules for each amino acid. The basic organization of each module is A-PCP-C. The A, or adenylation, region activates the domain's amino acid to allow transfer to the PCP, or peptide carrying protein, region. The activated amino acid is transferred to a cysteine residue in the PCP region, which anchors the amino acid and prepares the amino acid to be added to the polypeptide. The C, or condensation, region attaches the amino acid to the polypeptide. In addition, modules 2, 4, and 5 have E regions that epimerize (switch the stereochemistry) of the added amino acid to produce the correct configuration. Module 7, the last module, has an X and TE region. The X region is responsible for recruiting several of the tailoring enzymes that will perform the necessary reactions (halogenation, glycosylation, methylation, oxidative cross-linking, and hydroxylations) to produce chloroeremomycin. Finally, the TE, or thioesterase, region releases chloroeremomycin from the NRPS complex.