Illustration of conserved regions and predicted secondary structure of Actinomycetales Mce proteins. Six separate alignments of the Mce proteins (A-F) listed in Table 3 were submitted to JPred and the consensus secondary structure prediction estimated manually. White boxes represent α-helices and grey arrows β-strands. The C-terminal proline-rich region had low complexity and varied in length from 10–250 amino acids. Signal sequences were identified by SignalP and lipid attachment sites matched the ProSite motif PS00013.