coli, cysteine and glycine content, extinction coefficient, absorbance at 280 nm, absent and most prevalent amino acids, secondary (α-helix or β-strand) and tertiary structure (when available), physical method used for structural determination (e.g. NMR spectroscopy or X-ray diffraction) and critical residues for activity, whenever information was available. The Jmol applet http://​www.​jmol.​org was included for tertiary structure SHP099 supplier visualization. The statistical interface provides data on peptide sequence, function and structure. Data were analyzed

using selleck products SPSS software (version 17, SPSS Inc.) and medians and standard deviations were calculated. The following is a brief description of the database content. The current https://www.selleckchem.com/products/tucidinostat-chidamide.html release of the BACTIBASE dataset (version 2, July 2009) contains 177 (44% more) bacteriocin sequences, of which 156 are the products of Gram-positive organisms and 18 of Gram-negative organisms. We also note the presence of three bacteriocins from the Archaea domain. The database now comprises 31 genera, as shown in Table S1 (additional file 1). Without surprise, the lactic acid bacteria (order Lactobacillales) make up the predominant group of producers, with 113 bacteriocins. Figure 1 illustrates the distribution of peptide length among

the bacteriocins of Gram-positive organisms, which varies from 20 to 60 amino acids in 84% of cases. In contrast, Gram-negative bacteriocins come in a very broad range of lengths, the longest (BAC127) being 688 amino acid residues (data not shown). Amino acid percentages

are close to those calculated for the previous version of BACTIBASE. Table S1 lists averages for the net charge and amino acid contents of the bacteriocins produced by each of the 31 genera. These characteristics may serve as a physicochemical fingerprint for each group. Investigation of the PDB database revealed only 22 bacteriocins having Tangeritin a resolved 3D structure (by NMR spectroscopy or crystallography). Some of these are represented by more than one structure in the PDB database, bringing the total number of known 3D structures to 40. BACTIBASE provides detailed statistics on the bacteriocins. The improved database should be useful for discovering and characterizing potent bacteriocins or designing novel peptides with greater antimicrobial activity against pathogens. Figure 1 Peptide length distribution among the bacteriocins produced by the Gram-positive organisms in the BACTIBASE database. Utility Taxonomy explorer An integrated phylogenetic tree view was designed (Figure 2) to facilitate data retrieval via bacterial species name. The tree is displayed on the left and the corresponding bacteriocins are listed in tabled form on the right. In the default setting, the tree is collapsed and displays only the phyla assigned to the Bacteria and Archaea domains along with a brief definition of these in the table.