Exports Cu(+) from the cytoplasm to the periplasm (PubMed:10639134, PubMed:11167016, PubMed:11500054, PubMed:12351646). Binds 2 Cu(+) ions per monomer, which are transferred to periplasmic copper chaperone CusF upon ATP hydrolysis (PubMed:24917681). In vitro an excess of CusF over CopA is required for efficient transfer (PubMed:24917681). May also be involved in silver export (PubMed:12351646, PubMed:12832075). mRNA is subject to programmed ribosomal frameshifting which produces a cytoplasmic copper chaperone CopA(Z) that corresponds to the first HMA domain (PubMed:28107647). The soluble form is essential for cell survivial in the presence of CuSO(4); in growth competition experiments between wild-type and a version that prevents expression of CopA(Z) after 50 generations the non-CopA(Z) version is nearly extinct (PubMed:28107647). The first HMA domain (residues 1-70) can be replaced by B.subtilis Cu chaperone CopZ (PubMed:25899340). ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate Export is inhibited by vanadate (PubMed:10639134). Phosphorylation is inhibited by vanadate and sensitive to KOH and hydroxylamine; it is not inhibited by azide (PubMed:12351646). Phosphorylation is Cu(+) not Cu(2+)-dependent (PubMed:12351646). ATPase activity is inhibited by bathocuproindisulfonate (BCDS), which chelates Cu(+) but not Cu(2+), and stimulated 3-4-fold by Cu(+) (PubMed:12351646, PubMed:25899340). ATPase activity is inhibited by Cu(2+) plus DTT or Ag(+) (PubMed:12351646). Export tested with Isoform Copper-exporting P-type ATPase. Copper-exporting P-type ATPase interacts with apo-periplasmic copper chaperone CusF; when CusF is precharged with copper it binds very little CopA. The periplasmic loops of CopA, especially the first half of loop 1, play a large role in binding to CusF (PubMed:24917681). Induced by Cu(2+) and Ag(+) (at protein level) (PubMed:10639134). Transcriptionally regulated by CueR in response to Cu(+) or Ag(+) ions (PubMed:10639134, PubMed:11167016). Basal expression is low but unperturbed by disruption of cueR (PubMed:11167016). The N-terminal domain (exact residues are not given in the paper) is not required for Cu(+)-binding (when deleted KM for Cu(+) binding is 1.32 uM) nor for ATPase activity, binds 2 Cu(+)/monomer (PubMed:24917681). Contradictory results give a considerable decrease in Cu affinity when residues 1-150 are deleted (KM=31.9 uM for Cu(+)) (PubMed:25899340). The first of 2 N-terminal heavy metal-binding domains (HMA 1, approximately residues 1-70, equivalent to CopA(Z)) has a 5-fold higher affinity for Cu(+) than HMA 2 (residues 71-150) and as a protein fragment can transfer Cu(+) to the ATPase fragment (residues 151-834), suggesting it has a Cu-chaperone function (PubMed:25899340). HMA 2 transfers Cu(+) to HMA 1 but the opposite reaction does not occur in vitro (PubMed:25899340). The HMA 1 fragment complements growth defects in trans, but if its CXXC motif is mutated, or if the remaining CXXC motif in HMA2 is mutated, complementation no longer occurs, showing the 2 HMA domains have different functions (PubMed:25899340). The periplasmic loops of CopA, especially the first half of loop 1, play a large role in binding to CusF (PubMed:24917681). Contradictory results between the various in vitro studies may be due to different levels of protein expression or reconstitution (Probable). Decreased resistance to Cu(+) (PubMed:10639134, PubMed:11167016). No change in resistance to Zn(2+) or Cd(2+) (PubMed:10639134). Decreased resistance to AgNO(3) (PubMed:12832075). Increased intracellular levels of Cu(2+) (PubMed:11167016). Expression of the CopA(Z) soluble copper chaperone isoform requires a -1 programmed ribosomal frameshift (PRF) at the 70th codon, promoted by a nucleotide 'slippery sequence'. Silent mutations in the 'slippery sequence' abrogate expression of CopA(Z) but still allow expression of the full length protein. Both the mRNA secondary structure (a possible pseudoknot just downstream of the slippage site) and the sequence of the protein in the ribosomal exit tunnel modulate the efficiency of the -1 PRF (PubMed:28107647). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.