Similar to the extracellular lipolytic enzymes from the related genus Bacillus, Ala replaces the first Gly of the conserved Gly-X-Ser-X-Gly pentapeptide motif in PlpB [20]. Previous studies have reported Selleck STA-9090 that supplementing

the fermentation medium with fatty acids of various chain lengths enhanced the biosynthesis of lipopeptides containing selleck inhibitor specific fatty acid side chains [21, 22]. Thus, we speculated that the predicted extracellular lipase, PlpB, may facilitate the production of pelgipeptin through hydrolysis of water-soluble carboxyl esters in cultures of strain B69. The plpC gene encoded a predicted phosphopantetheinyl transferase The T domains of the PlpD-F must be converted from their inactive apo forms to cofactor-bearing

holo forms by a specific phosphopantetheinyl transferase via phosphopantetheinylation of thiotemplates. The product of the plpC gene might be responsible for this conversion. The deduced protein (244 amino acids) encoded by plpC showed high similarity to Sfp from B. subtilis (38% identity, 58% similarity), Gsp from B. brevis (37% identity, 54% similarity), Psf-1 from B. pumilus (35% identity, 55% similarity), and other phosphopantetheinyl www.selleckchem.com/products/bay80-6946.html transferases associated with non-ribosomal peptide synthetases. Further analysis indicated that PlpC fell within the W/KEA subfamily of Sfp-like phosphopantetheinyl transferases, which is involved in many kinds of secondary metabolite synthesis [23]. The N-terminal C domain The plp gene cluster contained a special C domain at the N terminus of PlpD (first C domain), in addition to eight typical C domains that presumably catalyzed peptide-bond formation between the adjacent amino acid residues of pelgipeptin. Sequence alignments shown that this first C domain of PlpD had only 19-25% identity with the remaining eight C domains of PlpD, -E, and –F, but shared 31-43% identity with other first C domains of lipopeptide synthetases, such as NRPSs of surfactin

[24], lichenysin [25], fengycin [26], fusaricidin [27] and polymyxin [12]. In the initiation reaction of the biosynthesis of surfactin, module 1 of SrfA alone was sufficient to catalyze the transfer of β-hydroxymyristoyl group to SrfA followed by formation of β-hydroxymyristoyl-glutamate [28]. The recent study of Choi’ Nintedanib (BIBF 1120) group also suggested that only the N-terminal C domain of PmxE was necessary for the fatty acyl tailing of polymyxin [12]. Thus, in the initial step of pelgipeptin biosynthesis, the PlpD N-terminal C domain was proposed to catalyze the condensation of the first amino acid (Dab) with a β-hydroxy fatty acid transferred from coenzyme A. Conclusions In the present study, we identified a potential pelgipeptin synthetase gene cluster (plp) in P. elgii B69 through genome analysis. The cluster spans 40.8 kb with three NRPS genes (plpD, plpE, and plpF).