@article{mbs:/content/journal/micro/10.1099/00221287-144-10-2837, author = "Metivier, Anita and Pilet, Marie-France and Dousset, Xavier and Sorokine, Odile and Anglade, Patricia and Zagorec, Monique and Piard, Jean-Christophe and Marlon, Didier and Cenatiempo, Yves and Fremaux, Christophe", title = "Divercin V41, a new bacteriocin with two disulphide bonds produced by Carnobacterium divergens V41: primary structure and genomic organization", journal= "Microbiology", year = "1998", volume = "144", number = "10", pages = "2837-2844", doi = "https://doi.org/10.1099/00221287-144-10-2837", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-144-10-2837", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "Carno6acterium", keywords = "lactic acid bacteria", keywords = "anti-listeria", keywords = "bacteriocin", abstract = "SUMMARY: Divercin V41 is a new bacteriocin produced by Carnobacterium divergens V41, a lactic acid bacterium isolated from fish viscera. The amino acid sequence of divercin V41 showed high homologies with pediocin PA-1 and enterocin A. Two disulphide bonds were present in the hydrophilic N-terminal domain and in the highly variable hydrophobic C-terminal domain, respectively. A DNA probe designed from the N-terminal sequence of the purified peptide was used to locate the structural gene of divercin V41. A 6 kb chromosomal fragment containing the divercin V41 structural gene (dvnA) was cloned and sequenced. The results indicate that divercin V41 is synthesized as a pre-bacteriocin of 66 amino acids. The 23-residue N-terminal extension is cleaved off t o yield the mature 43-amino-acid divercin V41. In addition, the fragment encodes putative proteins commonly found within bacteriocin operons, including an ATP- dependent transporter, two immunity-like proteins and the two components of a lantibiotic-type signal-transducing system. The genetic organization of the fragment suggested important gene rearrangements.", }