Skip to main content
. 2024 Jun 6;15(7):e01220-24. doi: 10.1128/mbio.01220-24

Fig 5.

A phylogenetic tree features the evolutionary relationships between the 32 different HTCS proteins from B. theta with RMSD values, conserved motif residues, and PULs with three 3D structures that compare the orientation of domains REC and DBD.

The conserved sequence motif correlates with the domain orientation in HTCSs from B. theta. (A) Comparison of predicted structures of HTCS-RR or HTCS-cyto with BT4124-RR. Sequences of the RR fragment of 32 HTCSs from B. theta were aligned with Clustal Omega to generate the phylogenetic tree using the neighbor-joining method and default parameters. RMSD values reflect the similarity of domain orientation to that of BT4124-RR. The “+” signs highlight the HTCSs that are within PULs involved in host glycan degradation (36). (B) Diverse domain orientations in HTCSs that have motif sequences that deviate from the consensus. Three representative HTCSs are shown. Predicted structures of other HTCSs, such as BT2391, BT2628, BT2971, and BT4236, are shown in Fig. S5 and S6.