Figure 5From: Diversity and evolution of the small multidrug resistance protein familyTM 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).Back to article page