Proteins up- and downstream of the putative duramycin biosynthetic gene cluster (Table S1); primary sequences of duramycin, duramycin B, duramycin C, cinnamycin, and cinnamycin B (Fig. S1); biosynthetic gene cluster for duramycin with extended putative ORFs located ca. 10 kb up- and downstream (Fig. S2); MALDI-TOF mass spectra of DurM-modified His6-DurA, of IAA assay of DurM-modified His6-DurA, of unmodified His6-DurA, and of IAA assay of unmodified His6-DurA (Fig. S3); liquid chromatography characterization of duramycin produced in E. coli BL21(DE3) (Fig. S4); antimicrobial agar diffusion growth assay of duramycin and derivatives against Bacillus subtilis ATCC 6633 (Fig. S5); isothermal titration calorimetry binding of PE to duramycin produced in E. coli after in vitro removal of the leader peptide by endoproteinase Glu-C and aminopeptidase (Fig. S6); MALDI-TOF mass spectra of DurM-modified His6-DurAduramycinC, of IAA assay of DurM-modified His6-DurAduramycinC, of unmodified His6-DurAduramycinC, and of IAA assay of unmodified His6-DurAduramycinC (Fig. S7); MALDI-TOF mass spectrum of His6-DurAduramycinC modified by DurM, DurN, and DurX (Fig. S8); isothermal titration calorimetry binding of PE to duramycin C produced in E. coli after in vitro removal of the leader peptide by Glu-C and aminopeptidase (Fig. S9); MALDI-TOF and ESI-Q-TOF mass spectra of DurX-modified His6-DurA followed by Glu-C cleavage (Fig. S10); MALDI-TOF mass spectra of DurM-modified His6-DurA mutants in E. coli (Fig. S11).
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