Sequence analyses of prominent virulence factors detected in the genome of C. ulcerans 809. (A), Analysis of the corynebacterial protease CP40 (Cpp). An amino acid sequence alignment of the corynebacterial proteases CP40 from C. pseudotuberculosis FRC41 and C. ulcerans 809 with the α domain of endoglycosidase EndoE from E. faecalis is shown. Predicted signal peptides are colored in yellow; predicted protein segments belonging to the α domain of EndoE are shaded gray. The catalytic FGH18 motif of EndoE is indicated by bold letters. The domain organization of EndoE is shown schematically below the sequence alignment. (B), Analysis of the corynebacterial ribosome-binding protein (Rbp). An amino acid sequence alignment of Rbp from C. ulcerans 809 with A chains of the Shiga-like toxins SLT-1 and SLT-2 from E. coli is shown. Conserved amino acids are highlighted in orange, while the conserved catalytic residues are highlighted in blue. The predicted signal peptide of Rbp is labeled yellow; the retranslocation domain of SLT-1 is marked as a green box. The similarity between Rbp and the A chain of SLT-1 is also shown as a 3-D model presented below the sequence alignment. Structural similarities between both proteins are indicated in red.
Trost et al. BMC Genomics 2011 12:383 doi:10.1186/1471-2164-12-383