Has bacteriocidal activity against some Gram-positive bacteria such as Listeria, some species of Bacillus and E.faecium (PubMed:10572140, PubMed:19633086, PubMed:3936839). A single mutation (Thr-14-Ile) confers hemolytic activity against rabbit and human blood (PubMed:19633086). The production of subtilosin A begins at the end of vegetative growth and finishes before spore formation. Transcription is highly induced by oxygen limitation and is under dual and independent control of Spo0A-AbrB and ResDE. This sactipeptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide (PubMed:12696888, PubMed:22366720). Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys-15 to Thr-36, and Cys-21 to Phe-30 (PubMed:12696888, PubMed:22366720). In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino acids (PubMed:12696888). Propeptide cleavage and cyclopeptide formation only occur after all 3 thioether cross-links are formed (PubMed:22366720). The Thr-14-Ile mutant. Belongs to the bacteriocin class V family. PubMed:3936839 sequence does not report residues in positions 30 and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence.