Fig. 3: New bacterial functions.

a Number of biosynthetic gene clusters (BGCs) identified within the novel taxa. NRPS non-ribosomal peptide synthetase, RiPP ribosomally synthesized and post-translationally modified peptides. b Top: consensus amino acid sequence of the PiBAC-derived sactipeptide-like BGCs with high sequence similarity in the precursor peptide sequence. Bottom: amino acid sequences of currently known sactipeptide natural products. Grey letters indicate amino acids of the leader peptides cleaved off in final products. Lines between bold amino acid residues indicate cyclization in the mature peptide. c Comparison of genetic organizations flanking the putative sactipeptide-like BGCs exemplarily shown for 15 of the pig strains. d Phylogenetic tree comparing amino acid sequences of known sactipeptide precursors (top six entries in red) and those from the pig bacteria. e Number of single CAZymes against CAZymes familes (top) and glycosyltransferases (GT) against GT families (bottom) for each member of the collection (n = 117 genomes representing 110 species depicted as dots). All data are provided in Supplementary Data 1. Orange dots indicate the 38 novel taxa while blue dots represent known bacterial species. Bacterial names correspond to species with the highest numbers of single enzymes or enzyme families. The position of Clostridium porci and Stecheria intestinalis is also shown (bottom), as these species encoded a GT of family 10 (along with Bacteroides fragilis). f Reaction of the new FucT from C. porci with N-acetyllactosamine. Top left box: HPLC measurements of the reaction without (negative control; top chromatogram) or with the co-substrate GDP-fucose (bottom). Relevant peaks (compounds) are named with letters: a, substrate (LacNAc type 2); b, target product; c, unidentified product with the same mass as the substrate and proposed to be iso-LacNAc, an isomer of LacNAc with a different bond between galactose and GlcNAc leading to a shift in retention time; likely originates from remnant transglycosidase activity in the enzyme preparation as also observed in the negative control. Right box: mass spectra of the relevant HPLC peaks. Bottom left box: putative reaction pathway catalyzed by C. porci.