Protein alignment of transmembrane segments 5 thru 8 of Cu/Ag or Zn/Cd/Pb – type P
-ATPases in Frankia. Transmembrane segments of Frankia heavy metal exporting ATPases (EC: 184.108.40.206 and 220.127.116.11) were aligned to identify amino acid changes that may alter metal specificity. Characterized ATPases from Escherichia coli K12-W3110 and those gene products that were up-regulated in the multiple array studies are included for comparison. Brackets indicate conserved amino acids that distinguish Cu/Ag - type from Zn/Cd/Pb - type ATPases. Asterisks indicate aspartate (D) and glutamate (E) amino acid residues in Frankia strains CN3 and DC12 that are potentially important for enhanced copper export. Amino acids are colored by characteristic: dark blue are negatively charged (D/E), purple are uncharged metal-binding (C/H), red are positively charged (K/R), pink are cyclic (P), orange are metal-binding and hydrophobic (M), yellow are hydrophobic (L/I/V/M/G/A), green are aromatic (F/W/Y), light blue are polar (S/T/N/Q).