Permease that is involved in the active transport across the cytoplasmic membrane of all three aromatic amino acids, phenylalanine, tyrosine and tryptophan. H(+)(in) + L-phenylalanine(in) = H(+)(out) + L-phenylalanine(out) H(+)(in) + L-tryptophan(in) = H(+)(out) + L-tryptophan(out) H(+)(in) + L-tyrosine(in) = H(+)(out) + L-tyrosine(out) Strong, mutual inhibition of uptake by tyrosine, phenylalanine, and tryptophan. Transport is also inhibited by the aromatic analogs p-fluorophenylalanine, beta-2-thienylalanine and 5-methyltryptophan. Contains three promoters, P1, P2 and P3 (PubMed:9209034, PubMed:9765583). Repressed by the regulatory protein TyrR, which binds to TyrR boxes (PubMed:9209034, PubMed:9765583, PubMed:14614536). In the absence of TyrR, the RNA polymerase (RNAP) has a higher affinity for P1 than for P2 and P3 and occupies the P1 promoter region (PubMed:9765583). When TyrR and its cofactors are present, TyrR inhibits the binding of RNA polymerase to the P1 promoter by recruiting RNA polymerase to the P3 promoter (PubMed:9765583). P1 is not repressed by TyrR alone but is repressed in the presence of phenylalanine, tyrosine or tryptophan (PubMed:9209034). P2 is partially repressed by TyrR alone and totally repressed by TyrR in the presence of tyrosine, phenylalanine or tryptophan (PubMed:9209034). Mutants show reduced aromatic amino acids transport and are resistant to p-fluorophenylalanine, beta-2-thienylalanine and 5-methyltryptophan. The general aromatic transport system is not essential for the supply of external aromatic amino acids to protein synthesis. Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.