Figure 2. Alignment of relevant amino acid sequences from selected MscS homologs. Sequence from archaeal (M. jannaschii), bacterial (E. coli, T. tengcongensis, C. glutamicum), algal (C. reinhardtii) and plant (A. thaliana) MscS homologs corresponding to TM2, TM3 and a portion of the middle-β domain were aligned with UGENE software (ugene.unipro.ru/). Bars in the bottom indicate the relevant domains from the EcMscS structure. Charged residues located at the end of TM2 and possibly affecting channel selectivity are in green, while the green star marks EcMscS R88. In the sequences that align with EcMscS TM3, hydrophobic residues are labeled gray, positively charged residues are labeled red and negatively charged residues are blue. The conservation of the pore constriction-forming residues from EcMscS, L105 and L109, is indicated with boxes.