Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:1368505, PubMed:9266851, PubMed:21889568). The trimodular NRPS acvA produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine (PubMed:9266851, PubMed:9355751, PubMed:19686863, PubMed:21889568). The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV (PubMed:8416970, PubMed:22777282). Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates (PubMed:9266851, PubMed:21889568). The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin in the peroxisomal matrix (PubMed:1368505) (Probable). 3 ATP + H2O + L-2-aminoadipate + L-cysteine + L-valine = 3 AMP + 3 diphosphate + 3 H(+) + N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine Binds 3 phosphopantetheines covalently. Optimum pH is 8.4. Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 1/3. Loosely attached to the vacuoles. Expression is repressed by glucose (PubMed:3096965). The transcription factor rfx1 controls penicillin biosynthesis through the regulation of the acvA, ipnA and aatA transcription (PubMed:22960281). The promoter heptameric sequence 5'-TTAGTAA-3' is the binding site for the transcriptional activator named penicillin transcriptional activator 1 (PTA1) (PubMed:10644695). Multiple additional DNA-binding proteins appear to bind to the promoter, including the nuclear factor A (NF-A) that recognizes an the 5'-GCCAAGCC-3' sequence or the global-acting nitrogen regulatory protein NIT2 that binds strongly at a single site that contains two closely spaced GATA sequences (PubMed:7614558). 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. GliP has the following architecture: A-T-C-A-T-C-A-T-E-TE. Belongs to the NRP synthetase family.