Fig. 4

Novel BGCs, encoding diverse lanthipeptide core sequences, consist of two LanMs for processing two types of precursor peptides. A Two BGCs encoding NHLP and N11P family lanthipeptide leaders in their precursor peptides with the corresponding synthetases, i.e. CHG motif and CCG motif LanM, were identified in Synechococcales. B Sequence logos of NHLP family and N11P family lanthipeptide leader sequences using the precursor sequences from the above two BGCs. C Sequence alignment of cyclase domain of putative LanMs from characteristic BGC of Synechococcales showed a difference in catalytic motif. RosM like LanMs has a CHG motif, while ProcM like LanMs have a CCG motif. D Sequence identity percentage in the pairwise alignment of the 12 lanthipeptide precursors’ leader sequences (lower half) and core sequences (upper half). Diversity among lanthipeptide core sequences was high, irrespective of leader conservation. E Multiple sequence alignment of lanthipeptide core sequences depicts natural diversity. LanA precursor peptide, LanM modification enzyme, HP Hypothetical Protein, LanT dual function peptidase-domain containing transporter