COPA_ECOLI
ID COPA_ECOLI Reviewed; 834 AA.
AC Q59385; A0A385XJA3; P78245; Q2MBU3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000303|PubMed:10639134};
DE EC=7.2.2.8 {ECO:0000305|PubMed:10639134, ECO:0000305|PubMed:24917681};
DE AltName: Full=Copper-exporting P-type ATPase A;
DE AltName: Full=Cu(+)-exporting ATPase;
DE AltName: Full=Soluble copper chaperone CopA(Z) {ECO:0000303|PubMed:28107647};
GN Name=copA {ECO:0000303|PubMed:10639134};
GN Synonyms=atcU {ECO:0000303|PubMed:9868784}, f834, ybaR;
GN OrderedLocusNames=b0484, JW0473;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Das S., Chuang E., Vulpe C., Goldman J., Gitschier J.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INDUCTION BY COPPER AND
RP SILVER, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911, and LMG194;
RX PubMed=10639134; DOI=10.1073/pnas.97.2.652;
RA Rensing C., Fan B., Sharma R., Mitra B., Rosen B.P.;
RT "CopA: an Escherichia coli Cu(I)-translocating P-type ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:652-656(2000).
RN [7]
RP FUNCTION, INDUCTION BY COPPER, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=11167016; DOI=10.1016/s0378-1119(00)00509-6;
RA Petersen C., Moeller L.B.;
RT "Control of copper homeostasis in Escherichia coli by a P-type ATPase,
RT CopA, and a MerR-like transcriptional activator, CopR.";
RL Gene 261:289-298(2000).
RN [8]
RP FUNCTION, MOTIF, AND MUTAGENESIS OF 8-THR--LEU-150; 14-CYS--CYS-17 AND
RP 110-CYS--CYS-113.
RC STRAIN=LMG194;
RX PubMed=11500054; DOI=10.1006/bbrc.2001.5367;
RA Fan B., Grass G., Rensing C., Rosen B.P.;
RT "Escherichia coli CopA N-terminal Cys(X)(2)Cys motifs are not required for
RT copper resistance or transport.";
RL Biochem. Biophys. Res. Commun. 286:414-418(2001).
RN [9]
RP FUNCTION IN TRANSPORT, FUNCTION AS AN ATPASE, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP 3-GLN--CYS-113; 7-LEU--GLU-54; 14-CYS--CYS-17; 110-CYS--CYS-113; CYS-479
RP AND CYS-481.
RC STRAIN=LMG194;
RX PubMed=12351646; DOI=10.1074/jbc.m208490200;
RA Fan B., Rosen B.P.;
RT "Biochemical characterization of CopA, the Escherichia coli Cu(I)-
RT translocating P-type ATPase.";
RL J. Biol. Chem. 277:46987-46992(2002).
RN [10]
RP FUNCTION IN SILVER EXPORT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=12832075; DOI=10.1016/s0014-5793(03)00640-9;
RA Stoyanov J.V., Magnani D., Solioz M.;
RT "Measurement of cytoplasmic copper, silver, and gold with a lux biosensor
RT shows copper and silver, but not gold, efflux by the CopA ATPase of
RT Escherichia coli.";
RL FEBS Lett. 546:391-394(2003).
RN [11]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [12]
RP FUNCTION AS AN ATPASE, FUNCTION IN TRANSFER TO CUSF, CATALYTIC ACTIVITY,
RP REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES, COPPER-BINDING, SUBUNIT,
RP DOMAIN, TOPOLOGY, AND MUTAGENESIS OF MET-204; 207-ASP--MET-210;
RP 212-THR--ARG-216; 273-TRP--PHE-277; 279-MET--HIS-283; GLU-287 AND
RP 797-TRP--THR-802.
RX PubMed=24917681; DOI=10.1074/jbc.m114.577668;
RA Padilla-Benavides T., George Thompson A.M., McEvoy M.M., Argueello J.M.;
RT "Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic
RT chaperones: the interaction of Escherichia coli CopA and CusF.";
RL J. Biol. Chem. 289:20492-20501(2014).
RN [13]
RP FUNCTION AS AN ATPASE, POSSIBLE CHAPERONE FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND MUTAGENESIS OF 1-MET--ALA-70;
RP 14-CYS--CYS-17 AND 110-CYS--CYS-113.
RC STRAIN=LMG194;
RX PubMed=25899340; DOI=10.1111/mmi.13038;
RA Drees S.L., Beyer D.F., Lenders-Lomscher C., Luebben M.;
RT "Distinct functions of serial metal-binding domains in the Escherichia coli
RT P1 B-ATPase CopA.";
RL Mol. Microbiol. 97:423-438(2015).
RN [14]
RP RIBOSOMAL FRAMESHIFT TO TRANSLATE ISOFORM SOLUBLE COPPER CHAPERONE COPA(Z),
RP AND FUNCTION AS A COPPER CHAPERONE.
RX PubMed=28107647; DOI=10.1016/j.molcel.2016.12.008;
RA Meydan S., Klepacki D., Karthikeyan S., Margus T., Thomas P., Jones J.E.,
RA Khan Y., Briggs J., Dinman J.D., Vazquez-Laslop N., Mankin A.S.;
RT "Programmed ribosomal frameshifting generates a copper transporter and a
RT copper chaperone from the same gene.";
RL Mol. Cell 65:207-219(2017).
CC -!- FUNCTION: [Copper-exporting P-type ATPase]: Exports Cu(+) from the
CC cytoplasm to the periplasm (PubMed:10639134, PubMed:11167016,
CC PubMed:11500054, PubMed:12351646). Binds 2 Cu(+) ions per monomer,
CC which are transferred to periplasmic copper chaperone CusF upon ATP
CC hydrolysis (PubMed:24917681). In vitro an excess of CusF over CopA is
CC required for efficient transfer (PubMed:24917681). May also be involved
CC in silver export (PubMed:12351646, PubMed:12832075).
CC {ECO:0000269|PubMed:10639134, ECO:0000269|PubMed:11167016,
CC ECO:0000269|PubMed:11500054, ECO:0000269|PubMed:12351646,
CC ECO:0000269|PubMed:12832075, ECO:0000269|PubMed:24917681}.
CC -!- FUNCTION: [Isoform Soluble copper chaperone CopA(Z)]: mRNA is subject
CC to programmed ribosomal frameshifting which produces a cytoplasmic
CC copper chaperone CopA(Z) that corresponds to the first HMA domain
CC (PubMed:28107647). The soluble form is essential for cell survivial in
CC the presence of CuSO(4); in growth competition experiments between
CC wild-type and a version that prevents expression of CopA(Z) after 50
CC generations the non-CopA(Z) version is nearly extinct
CC (PubMed:28107647). The first HMA domain (residues 1-70) can be replaced
CC by B.subtilis Cu chaperone CopZ (PubMed:25899340).
CC {ECO:0000269|PubMed:25899340, ECO:0000269|PubMed:28107647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000305|PubMed:10639134, ECO:0000305|PubMed:24917681};
CC -!- ACTIVITY REGULATION: [Copper-exporting P-type ATPase]: Export is
CC inhibited by vanadate (PubMed:10639134). Phosphorylation is inhibited
CC by vanadate and sensitive to KOH and hydroxylamine; it is not inhibited
CC by azide (PubMed:12351646). Phosphorylation is Cu(+) not Cu(2+)-
CC dependent (PubMed:12351646). ATPase activity is inhibited by
CC bathocuproindisulfonate (BCDS), which chelates Cu(+) but not Cu(2+),
CC and stimulated 3-4-fold by Cu(+) (PubMed:12351646, PubMed:25899340).
CC ATPase activity is inhibited by Cu(2+) plus DTT or Ag(+)
CC (PubMed:12351646). {ECO:0000269|PubMed:10639134,
CC ECO:0000269|PubMed:12351646, ECO:0000269|PubMed:25899340}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for copper {ECO:0000269|PubMed:12351646};
CC KM=0.5 mM for ATP {ECO:0000269|PubMed:12351646};
CC KM=1.48 uM for Cu(+) {ECO:0000269|PubMed:24917681};
CC KM=5.4 uM for Cu(+) {ECO:0000269|PubMed:25899340};
CC Vmax=0.19 umol/min/mg enzyme (in the presence of CuCl(2) and 1 mM
CC DTT) {ECO:0000269|PubMed:12351646};
CC Vmax=1.64 umol/h/mg enzyme for Cu(+) {ECO:0000269|PubMed:24917681};
CC Note=Export tested with Isoform Copper-exporting P-type ATPase.
CC {ECO:0000305};
CC -!- SUBUNIT: Copper-exporting P-type ATPase interacts with apo-periplasmic
CC copper chaperone CusF; when CusF is precharged with copper it binds
CC very little CopA. The periplasmic loops of CopA, especially the first
CC half of loop 1, play a large role in binding to CusF (PubMed:24917681).
CC {ECO:0000269|PubMed:24917681}.
CC -!- SUBCELLULAR LOCATION: [Copper-exporting P-type ATPase]: Cell inner
CC membrane {ECO:0000269|PubMed:15919996, ECO:0000305|PubMed:12351646};
CC Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
CC -!- SUBCELLULAR LOCATION: [Isoform Soluble copper chaperone CopA(Z)]:
CC Cytoplasm {ECO:0000305|PubMed:28107647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Copper-exporting P-type ATPase;
CC IsoId=Q59385-1; Sequence=Displayed;
CC Name=Soluble copper chaperone CopA(Z);
CC IsoId=Q59385-2; Sequence=VSP_059176;
CC -!- INDUCTION: [Copper-exporting P-type ATPase]: Induced by Cu(2+) and
CC Ag(+) (at protein level) (PubMed:10639134). Transcriptionally regulated
CC by CueR in response to Cu(+) or Ag(+) ions (PubMed:10639134,
CC PubMed:11167016). Basal expression is low but unperturbed by disruption
CC of cueR (PubMed:11167016). {ECO:0000269|PubMed:10639134,
CC ECO:0000269|PubMed:11167016}.
CC -!- DOMAIN: The N-terminal domain (exact residues are not given in the
CC paper) is not required for Cu(+)-binding (when deleted KM for Cu(+)
CC binding is 1.32 uM) nor for ATPase activity, binds 2 Cu(+)/monomer
CC (PubMed:24917681). Contradictory results give a considerable decrease
CC in Cu affinity when residues 1-150 are deleted (KM=31.9 uM for Cu(+))
CC (PubMed:25899340). The first of 2 N-terminal heavy metal-binding
CC domains (HMA 1, approximately residues 1-70, equivalent to CopA(Z)) has
CC a 5-fold higher affinity for Cu(+) than HMA 2 (residues 71-150) and as
CC a protein fragment can transfer Cu(+) to the ATPase fragment (residues
CC 151-834), suggesting it has a Cu-chaperone function (PubMed:25899340).
CC HMA 2 transfers Cu(+) to HMA 1 but the opposite reaction does not occur
CC in vitro (PubMed:25899340). The HMA 1 fragment complements growth
CC defects in trans, but if its CXXC motif is mutated, or if the remaining
CC CXXC motif in HMA2 is mutated, complementation no longer occurs,
CC showing the 2 HMA domains have different functions (PubMed:25899340).
CC The periplasmic loops of CopA, especially the first half of loop 1,
CC play a large role in binding to CusF (PubMed:24917681). Contradictory
CC results between the various in vitro studies may be due to different
CC levels of protein expression or reconstitution (Probable).
CC {ECO:0000269|PubMed:24917681, ECO:0000269|PubMed:25899340,
CC ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Decreased resistance to Cu(+) (PubMed:10639134,
CC PubMed:11167016). No change in resistance to Zn(2+) or Cd(2+)
CC (PubMed:10639134). Decreased resistance to AgNO(3) (PubMed:12832075).
CC Increased intracellular levels of Cu(2+) (PubMed:11167016).
CC {ECO:0000269|PubMed:10639134, ECO:0000269|PubMed:11167016,
CC ECO:0000269|PubMed:12832075}.
CC -!- MISCELLANEOUS: [Isoform Soluble copper chaperone CopA(Z)]: Expression
CC of the CopA(Z) soluble copper chaperone isoform requires a -1
CC programmed ribosomal frameshift (PRF) at the 70th codon, promoted by a
CC nucleotide 'slippery sequence'. Silent mutations in the 'slippery
CC sequence' abrogate expression of CopA(Z) but still allow expression of
CC the full length protein. Both the mRNA secondary structure (a possible
CC pseudoknot just downstream of the slippage site) and the sequence of
CC the protein in the ribosomal exit tunnel modulate the efficiency of the
CC -1 PRF (PubMed:28107647). {ECO:0000305|PubMed:28107647}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; U58330; AAB02268.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40238.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73586.1; -; Genomic_DNA.
DR EMBL; U00096; AYC08180.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76263.1; -; Genomic_DNA.
DR PIR; C64779; C64779.
DR RefSeq; NP_415017.1; NC_000913.3.
DR RefSeq; WP_000083955.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; Q59385; -.
DR SMR; Q59385; -.
DR BioGRID; 4261336; 115.
DR IntAct; Q59385; 6.
DR STRING; 511145.b0484; -.
DR TCDB; 3.A.3.5.5; the p-type atpase (p-atpase) superfamily.
DR jPOST; Q59385; -.
DR PaxDb; Q59385; -.
DR PRIDE; Q59385; -.
DR EnsemblBacteria; AAC73586; AAC73586; b0484.
DR EnsemblBacteria; AYC08180; AYC08180; b0484.
DR EnsemblBacteria; BAE76263; BAE76263; BAE76263.
DR GeneID; 946106; -.
DR KEGG; ecj:JW0473; -.
DR KEGG; eco:b0484; -.
DR PATRIC; fig|1411691.4.peg.1792; -.
DR EchoBASE; EB3035; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_6; -.
DR InParanoid; Q59385; -.
DR OMA; ITFFGWM; -.
DR PhylomeDB; Q59385; -.
DR BRENDA; 7.2.2.8; 2026.
DR SABIO-RK; Q59385; -.
DR PRO; PR:Q59385; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoliWiki.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0015662; F:P-type ion transporter activity; IDA:EcoCyc.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0015080; F:silver ion transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0071280; P:cellular response to copper ion; IEP:EcoCyc.
DR GO; GO:0071292; P:cellular response to silver ion; IEP:EcoCyc.
DR GO; GO:0060003; P:copper ion export; IDA:EcoCyc.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0006825; P:copper ion transport; IMP:EcoliWiki.
DR GO; GO:0010273; P:detoxification of copper ion; IDA:EcoCyc.
DR GO; GO:1902601; P:silver ion transmembrane transport; IMP:EcoCyc.
DR CDD; cd00371; HMA; 2.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 2.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 2.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Chaperone; Copper;
KW Copper transport; Cytoplasm; Direct protein sequencing; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ribosomal frameshifting; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9868784"
FT CHAIN 2..834
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000046320"
FT TOPO_DOM 2..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..217
FT /note="Periplasmic; loop 1"
FT /evidence="ECO:0000305|PubMed:24917681"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..283
FT /note="Periplasmic; loop 2"
FT /evidence="ECO:0000305|PubMed:24917681"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..463
FT /note="Periplasmic; loop 3"
FT /evidence="ECO:0000305"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800
FT /note="Periplasmic; loop 4"
FT /evidence="ECO:0000305|PubMed:24917681"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 3..64
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 99..162
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MOTIF 14..17
FT /note="CXXC motif 1"
FT /evidence="ECO:0000305|PubMed:11500054"
FT MOTIF 110..113
FT /note="CXXC motif 2"
FT /evidence="ECO:0000305|PubMed:11500054"
FT ACT_SITE 523
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305|PubMed:12351646"
FT BINDING 14
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 17
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 110
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 113
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 724
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT VAR_SEQ 70..834
FT /note="AKPLAESSIPSEALTAVSEALPAATADDDDSQQLLLSGMSCASCVTRVQNAL
FT QSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYGAEAIEDDAKRRERQQETAVA
FT TMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYR
FT SAWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINL
FT GHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPV
FT DGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRII
FT RMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVL
FT IIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQ
FT VVAVKTFADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQLPQVNGFRTLRGLGVSG
FT EAEGHALLLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLR
FT SDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSE
FT GRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRAT
FT LHNMKQNLLGAFIYNSIGIPVAAGILWPFTGTLLNPVVAGAAMALSSITVVSNANRLLR
FT FKPKE -> G (in isoform Soluble copper chaperone CopA(Z))"
FT /evidence="ECO:0000305|PubMed:28107647"
FT /id="VSP_059176"
FT MUTAGEN 1..70
FT /note="Missing: Slight increase in CuSO(4)-stimulation of
FT ATPase, no growth in CuSO(4). Grows when this protein
FT fragment is provided in trans or if B.subtilis CopZ is
FT present."
FT /evidence="ECO:0000269|PubMed:25899340"
FT MUTAGEN 3..113
FT /note="Missing: No resistance to CuSO(4), does not form
FT phosphate intermediate."
FT /evidence="ECO:0000269|PubMed:12351646"
FT MUTAGEN 7..54
FT /note="Missing: Partial resistance to CuSO(4), forms
FT phosphate intermediate."
FT /evidence="ECO:0000269|PubMed:12351646"
FT MUTAGEN 8..150
FT /note="Missing: Loss of growth in the presence of CuSO(4),
FT loss of Cu efflux."
FT /evidence="ECO:0000269|PubMed:11500054"
FT MUTAGEN 14..17
FT /note="CGHC->AGHA: Wild-type growth in the presence of
FT CuSO(4), no change in Cu efflux. Still forms phosphate
FT intermediate; when associated with 110-A--A-113."
FT /evidence="ECO:0000269|PubMed:11500054,
FT ECO:0000269|PubMed:12351646"
FT MUTAGEN 14..17
FT /note="CGHC->SGHS: No change in CuSO(4)-stimulation of
FT ATPase. When expressed as an isolated protein fragment
FT (residues 1-70) does not restore growth to the 71-K--G-834
FT fragment."
FT /evidence="ECO:0000269|PubMed:25899340"
FT MUTAGEN 32..67
FT /note="EQADVSITEAHVTGTASAEQLIETIKQAGYDASVSH->SRRMCLSLKRTLPG
FT LPVQNSRSKPSNKRVMTHLYAN: Reduces -1 frameshifting efficiency
FT about 2-fold in a 104 residue truncated construct."
FT /evidence="ECO:0000269|PubMed:28107647"
FT MUTAGEN 110..113
FT /note="CASC->AASA: Wild-type growth in the presence of
FT CuSO(4), no change in Cu efflux. Still forms phosphate
FT intermediate; when associated with 14-A--A-17."
FT /evidence="ECO:0000269|PubMed:11500054,
FT ECO:0000269|PubMed:12351646"
FT MUTAGEN 110..113
FT /note="CASC->SASS: Loss of CuSO(4)-stimulation of ATPase.
FT When present in the 51-K--G-834 fragment growth in CuSO(4)
FT is not restored by protein fragment 1-M--A-70."
FT /evidence="ECO:0000269|PubMed:25899340"
FT MUTAGEN 204
FT /note="M->A: Decreased transfer of Cu(+) to CusF, binds 2
FT Cu(+)."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 207..210
FT /note="DNMM->AAAA: First half of periplasmic loop 1,
FT transfers about 10% Cu(+) to CusF."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 212..216
FT /note="TADNR->AAANA: Second half of periplasmic loop 1,
FT wild-type transfer of Cu(+) to CusF."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 273..277
FT /note="WPQWF->APQAA: First half of periplasmic loop 2,
FT nearly wild-type transfer of Cu(+) to CusF."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 279..283
FT /note="MEARH->AAARA: Second half of periplasmic loop 2,
FT wild-type transfer of Cu(+) to CusF."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 287
FT /note="E->A: Decreased transfer of Cu(+) to CusF."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 479
FT /note="C->A: Loss of copper resistance, transport and
FT phosphoenzyme formation."
FT /evidence="ECO:0000269|PubMed:12351646"
FT MUTAGEN 481
FT /note="C->A,H: Loss of copper resistance, transport and
FT phosphoenzyme formation."
FT /evidence="ECO:0000269|PubMed:12351646"
FT MUTAGEN 797..802
FT /note="WPFTGT->APFAGA: Periplasmic loop 4, nearly wild-type
FT transfer of Cu(+) to CusF."
FT /evidence="ECO:0000269|PubMed:24917681"
FT CONFLICT 162..181
FT /note="EAIEDDAKRRERQQETAVAT -> KRLKMTLNAASASKKPPSLA (in
FT Ref. 1; AAB02268)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="A -> R (in Ref. 1; AAB02268)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="Q -> R (in Ref. 1; AAB02268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 87873 MW; CF84A18FE208E6F6 CRC64;
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG
YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA
LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA
TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS
AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE
ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR
QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP
CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT
FADVDEAQAL RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL
LLGNQALLNE QQVGTKAIEA EITAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ
RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKHLQS EGRQVAMVGD
GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LHNMKQNLLG
AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE
