BACTIBASE: a new web-accessible database for bacteriocin characterization

In the present paper, we present the development of a new and original database BACTIBASE that contains calculated or predicted physicochemical properties of 123 bacteriocins produced by both Gram-positive and Gram-negative bacteria. The information in this database is very easy to extract and allows rapid prediction of relationships structure/function and target organisms of these peptides and therefore better exploitation of their biological activity in both the medical and food sectors.The BACTIBASE database is freely available at http://bactibase.pfba-lab.org webcite, web-based platform enabling easy retrieval, via various filters, of sets of bacteriocins that will enable detailed analysis of a number of microbiological and physicochemical data.Bacteriocins are antimicrobial peptides produced by many bacteria and display inhibitory activity against closely related bacteria [1]. Bacteriocin production in some bacteria is regulated by a widespread mechanism of the quorum sensing type that appears to play a major role in monitoring the cell density of a bacterial population in a given environment [2].Since their discovery by [3] in 1925, nearly 300 bacteriocins have been identified and some of them have been used successfully for inhibiting both animal and human pathogens [4,5]. A few of these have been well characterized and information such as amino acid sequence and spectra of antimicrobial activity are now available. However, for many other bacteriocins, this kind of information is still missing or is scattered in the scientific literature and therefore unavailable to potential users. This situation could be improved by a central resource such as a database in which data could be collected, analyzed and used to generate new and useful information.The majority of sequenced bacteriocins are stored in the manually annotated UniProtKB/Swiss-Prot database and relevant data are available as information about mode of action, 3D-structure data, post-translationally mod