Figure 5

TM domain alignments of SMR proteins to drug and metabolite transporters from BAT and DMT protein families. Protein alignments were performed using ClustalW and manual editing using GeneDoc (v 2.5.010 [64]). Artificial fusions proteins of all SMR proteins from each subclass were performed (data not shown) and selected alignments for the fused protein pairs Eco-YdgF to Eco-YdgE and Eco-EmrE to Eco-SugE are shown in panel B. TM domains for SMR proteins are highlighted in red whereas all other predicted TM domains are highlighted in blue. M residues are boxed in red in each alignment in both panels to indicate the starting residue for SMR fusion sequences. Conserved residues at a given position within TM domains are indicated by the amino acid letter below the sequence and moderate to high amino acid similarity is indicated by a single or two dots respectively at each position. Panel A indicates the alignment of Eco-SugE and Eco-EmrE sequences to predicted TM domains of BAT family proteins from Archaeal Aquifex aeolicus (AAC07598; 143 a.a.) and Bacterial Neisseria meningitidis (AAF42175; 143 a.a.). Panel B shows alignments of Eco-EmrE to Eco-SugE and Eco-YdgF to Eco-YdgF fusions is aligned with the DMT superfamily members E. coli RarD (ZP_03000057; 286 a.a.) and Salmonella enterica PagO (ZP_03162845; 304 a.a).