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Summary  Powered by  ATP  hydrolysis,  P IB  ‐ ATPases  drive the energetically uphill transport of transition metals. These high affinity pumps are essential for heavy metal detoxification and delivery of metal cofactors to specific cellular compartments. Amino acid sequence alignment of the trans‐membrane ( TM ) helices of  P IB  ‐ ATPases  reveals a high degree of conservation, with ∼60–70 fully conserved positions. Of these conserved positions, 6–7 were previously identified to be important for transport. However, the functional importance of the majority of the conserved  TM  residues remains unclear. To investigate the role of conserved  TM  residues of  P IB  ‐ ATPases  we conducted an extensive mutagenesis study of a   Zn 2+   /  Cd 2+   P IB  ‐ ATPase  from   R   hizobium radiobacter  ( rrZntA ) and seven other  P IB  ‐ ATPases . Of the 38 conserved positions tested, 24 had small effects on metal tolerance. Fourteen mutations compromised  in vivo  metal tolerance and  in vitro  metal‐stimulated  ATPase  activity. Based on structural modelling, the functionally important residues line a constricted ‘channel’, tightly surrounded by the residues that were found to be inconsequential for function. We tentatively propose that the distribution of the mutable and immutable residues marks a possible trans‐membrane metal translocation pathway. In addition, by substituting six trans‐membrane amino acids of  rrZntA  we changed the  in vivo  metal specificity of this pump from   Zn 2+   /  Cd 2+    to   Ag +   .

Identification of functionally important conserved trans‐membrane residues of bacterial P IB ‐type ATPases