Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins (PubMed:28376389). 11'-deoxyverticillin A is required for normal conidiation (PubMed:28376389). The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable). Mycotoxin biosynthesis. Expression is regulated by the cluster-specific regulator verZ. 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. VerP has the following architecture: A-T-C-A-T-C. Completely abolishes the 11'-deoxyverticillin A production and conidiation. Belongs to the NRP synthetase family.