The formation of Lan and MeLan are attributed to the intermolecular cyclization of the thiol groups of cysteine residues with Dha and Dhb, which are obtained from the dehydration of serine and threonine residues, respectively. Dedicated biosynthetic enzymes are required during the process of maturation and the genes encoding these proteins are clustered, as described for nisin [4, 5], pep5

[6], nukacin ISK-1 [7], epicidin 280 [8], and mersacidin [9]. According to the genetic organization of lantibiotics, they can be divided into several types [10, 11]. The typical gene cluster of type AI lantibiotics, such as nisin and epidermin, includes the structural gene lanA, modification enzyme-encoding genes lanB and lanC, find more the processing protease-encoding gene lanP, the transporter gene lanT, and the immunity genes lanI and/or lanEFG. However, not all type AI lantibiotic-like

gene clusters contain all these genes; for example, in the gene cluster spaBTCAIFGRK [12], which codes for the biosynthesis of subtilin, the function of LanP is replaced by an intrinsic protease of Bacillus subtilis ATCC 6633 [13]. Much attention has been concentrated on the identification of new lantibiotics because of their potent antimicrobial activities. In recent years, with the availability of abundant genomic sequence data in public databases, many new lantibiotics and lantipeptides such as Bsa, lichenicidin, selleck chemicals llc and a range of cyanobacteria-associated lantipeptides [14–16] have been identified. For example, the bacterial genus Paenibacillus MG 132 is known for its ability to produce peptide antibiotics [17–19], and an increasing this website number of Paenibacillus spp. genomes have been sequenced, revealing several novel lantibiotic-related gene clusters [20, 21]. However, to date, only one novel lantibiotic, paenibacillin,

produced by Paenibacillus polymyxa OSY-DF [22] has been reported. In the present study, we present the detailed bioinformatic analysis of a novel lantibiotic-like gene cluster in the Paenibacillus elgii B69 genome. Screening of bacterial cultures, mass spectrometry (MS) analysis, and N-terminal amino acid sequencing were used to confirm that the P. elgii B69 gene cluster encodes elgicins, novel broad-spectrum lantibiotics. Results and discussion Putative lantibiotic-like gene cluster of P. Elgii B69 P. elgii B69 was subjected to whole-genome shotgun sequencing, yielding 7.9 Mb of sequence on 278 assembled contigs [23]. Data mining for the LanC homolog amidst the genomic data of P. elgii B69, using the SpaC sequence of P. polymyxa E681 as a driver, resulted in the identification of a lantibiotic-like gene cluster containing five probable open reading frames (ORFs), designated elgT1, elgC, elgT2, elgB, and elgA (Figure 1A).