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Copper-exporting P-type ATPase (EC 3.6.3.54) (Copper-exporting P-type ATPase A) (Cu( )-exporting ATPase) (Soluble copper chaperone CopA(Z))

 COPA_ECOLI              Reviewed;         834 AA.
Q59385; P78245; Q2MBU3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 160.
RecName: Full=Copper-exporting P-type ATPase {ECO:0000303|PubMed:10639134};
EC=3.6.3.54 {ECO:0000305|PubMed:10639134, ECO:0000305|PubMed:24917681};
AltName: Full=Copper-exporting P-type ATPase A;
AltName: Full=Cu(+)-exporting ATPase;
AltName: Full=Soluble copper chaperone CopA(Z) {ECO:0000303|PubMed:28107647};
Name=copA {ECO:0000303|PubMed:10639134};
Synonyms=atcU {ECO:0000303|PubMed:9868784}, f834, ybaR;
OrderedLocusNames=b0484, JW0473;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Das S., Chuang E., Vulpe C., Goldman J., Gitschier J.;
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-11.
STRAIN=K12;
PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
Wasinger V.C., Humphery-Smith I.;
"Small genes/gene-products in Escherichia coli K-12.";
FEMS Microbiol. Lett. 169:375-382(1998).
[6]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INDUCTION BY COPPER
AND SILVER, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911, and LMG194;
PubMed=10639134; DOI=10.1073/pnas.97.2.652;
Rensing C., Fan B., Sharma R., Mitra B., Rosen B.P.;
"CopA: an Escherichia coli Cu(I)-translocating P-type ATPase.";
Proc. Natl. Acad. Sci. U.S.A. 97:652-656(2000).
[7]
FUNCTION, INDUCTION BY COPPER, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=11167016; DOI=10.1016/S0378-1119(00)00509-6;
Petersen C., Moeller L.B.;
"Control of copper homeostasis in Escherichia coli by a P-type ATPase,
CopA, and a MerR-like transcriptional activator, CopR.";
Gene 261:289-298(2000).
[8]
FUNCTION, MOTIF, AND MUTAGENESIS OF 8-THR--LEU-150; 14-CYS--CYS-17 AND
110-CYS--CYS-113.
STRAIN=LMG194;
PubMed=11500054; DOI=10.1006/bbrc.2001.5367;
Fan B., Grass G., Rensing C., Rosen B.P.;
"Escherichia coli CopA N-terminal Cys(X)(2)Cys motifs are not required
for copper resistance or transport.";
Biochem. Biophys. Res. Commun. 286:414-418(2001).
[9]
FUNCTION IN TRANSPORT, FUNCTION AS AN ATPASE, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, PHOSPHORYLATION, AND MUTAGENESIS OF
3-GLN--CYS-113; 7-LEU--GLU-54; 14-CYS--CYS-17; 110-CYS--CYS-113;
CYS-479 AND CYS-481.
STRAIN=LMG194;
PubMed=12351646; DOI=10.1074/jbc.M208490200;
Fan B., Rosen B.P.;
"Biochemical characterization of CopA, the Escherichia coli Cu(I)-
translocating P-type ATPase.";
J. Biol. Chem. 277:46987-46992(2002).
[10]
FUNCTION IN SILVER EXPORT, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=12832075; DOI=10.1016/S0014-5793(03)00640-9;
Stoyanov J.V., Magnani D., Solioz M.;
"Measurement of cytoplasmic copper, silver, and gold with a lux
biosensor shows copper and silver, but not gold, efflux by the CopA
ATPase of Escherichia coli.";
FEBS Lett. 546:391-394(2003).
[11]
SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[12]
FUNCTION AS AN ATPASE, FUNCTION IN TRANSFER TO CUSF, CATALYTIC
ACTIVITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES,
COPPER-BINDING, SUBUNIT, DOMAIN, TOPOLOGY, AND MUTAGENESIS OF MET-204;
207-ASP--MET-210; 212-THR--ARG-216; 273-TRP--PHE-277;
279-MET--HIS-283; GLU-287 AND 797-TRP--THR-802.
PubMed=24917681; DOI=10.1074/jbc.M114.577668;
Padilla-Benavides T., George Thompson A.M., McEvoy M.M.,
Argueello J.M.;
"Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic
chaperones: the interaction of Escherichia coli CopA and CusF.";
J. Biol. Chem. 289:20492-20501(2014).
[13]
FUNCTION AS AN ATPASE, POSSIBLE CHAPERONE FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND MUTAGENESIS OF
1-MET--ALA-70; 14-CYS--CYS-17 AND 110-CYS--CYS-113.
STRAIN=LMG194;
PubMed=25899340; DOI=10.1111/mmi.13038;
Drees S.L., Beyer D.F., Lenders-Lomscher C., Luebben M.;
"Distinct functions of serial metal-binding domains in the Escherichia
coli P1 B-ATPase CopA.";
Mol. Microbiol. 97:423-438(2015).
[14]
RIBOSOMAL FRAMESHIFT TO TRANSLATE ISOFORM SOLUBLE COPPER CHAPERONE
COPA(Z), AND FUNCTION AS A COPPER CHAPERONE.
PubMed=28107647; DOI=10.1016/j.molcel.2016.12.008;
Meydan S., Klepacki D., Karthikeyan S., Margus T., Thomas P.,
Jones J.E., Khan Y., Briggs J., Dinman J.D., Vazquez-Laslop N.,
Mankin A.S.;
"Programmed ribosomal frameshifting generates a copper transporter and
a copper chaperone from the same gene.";
Mol. Cell 65:207-219(2017).
-!- FUNCTION: Copper-exporting P-type ATPase: 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). {ECO:0000269|PubMed:10639134,
ECO:0000269|PubMed:11167016, ECO:0000269|PubMed:11500054,
ECO:0000269|PubMed:12351646, ECO:0000269|PubMed:12832075,
ECO:0000269|PubMed:24917681}.
-!- FUNCTION: Soluble copper chaperone CopA(Z): 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). {ECO:0000269|PubMed:25899340,
ECO:0000269|PubMed:28107647}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate
+ Cu(+)(Side 2). {ECO:0000305|PubMed:10639134,
ECO:0000305|PubMed:24917681}.
-!- ENZYME REGULATION: Copper-exporting P-type ATPase: 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). {ECO:0000269|PubMed:10639134,
ECO:0000269|PubMed:12351646, ECO:0000269|PubMed:25899340}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.5 uM for copper {ECO:0000269|PubMed:12351646};
KM=0.5 mM for ATP {ECO:0000269|PubMed:12351646};
KM=1.48 uM for Cu(+) {ECO:0000269|PubMed:24917681};
KM=5.4 uM for Cu(+) {ECO:0000269|PubMed:25899340};
Vmax=0.19 umol/min/mg enzyme (in the presence of CuCl(2) and 1
mM DTT) {ECO:0000269|PubMed:12351646};
Vmax=1.64 umol/h/mg enzyme for Cu(+)
{ECO:0000269|PubMed:24917681};
Note=Export tested with Isoform Copper-exporting P-type ATPase.
{ECO:0000305};
-!- SUBUNIT: 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). {ECO:0000269|PubMed:24917681}.
-!- SUBCELLULAR LOCATION: Copper-exporting P-type ATPase: Cell inner
membrane {ECO:0000269|PubMed:15919996,
ECO:0000305|PubMed:12351646}; Multi-pass membrane protein
{ECO:0000305|PubMed:15919996}.
-!- SUBCELLULAR LOCATION: Isoform Soluble copper chaperone CopA(Z):
Cytoplasm {ECO:0000305|PubMed:28107647}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Copper-exporting P-type ATPase;
IsoId=Q59385-1; Sequence=Displayed;
Name=Soluble copper chaperone CopA(Z);
IsoId=Q59385-2; Sequence=VSP_059176;
Note=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 (Ref.14). {ECO:0000305|PubMed:28107647};
-!- INDUCTION: Copper-exporting P-type ATPase: 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).
{ECO:0000269|PubMed:10639134, ECO:0000269|PubMed:11167016}.
-!- DOMAIN: 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
tranfers 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). {ECO:0000269|PubMed:24917681,
ECO:0000269|PubMed:25899340, ECO:0000305}.
-!- DISRUPTION PHENOTYPE: 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). {ECO:0000269|PubMed:10639134,
ECO:0000269|PubMed:11167016, ECO:0000269|PubMed:12832075}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
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EMBL; U58330; AAB02268.1; -; Genomic_DNA.
EMBL; U82664; AAB40238.1; -; Genomic_DNA.
EMBL; U00096; AAC73586.1; -; Genomic_DNA.
EMBL; AP009048; BAE76263.1; -; Genomic_DNA.
PIR; C64779; C64779.
RefSeq; NP_415017.1; NC_000913.3.
RefSeq; WP_000083955.1; NZ_LN832404.1.
ProteinModelPortal; Q59385; -.
SMR; Q59385; -.
BioGrid; 4261336; 9.
IntAct; Q59385; 6.
STRING; 316385.ECDH10B_0441; -.
TCDB; 3.A.3.5.5; the p-type atpase (p-atpase) superfamily.
PaxDb; Q59385; -.
PRIDE; Q59385; -.
EnsemblBacteria; AAC73586; AAC73586; b0484.
EnsemblBacteria; BAE76263; BAE76263; BAE76263.
GeneID; 946106; -.
KEGG; ecj:JW0473; -.
KEGG; eco:b0484; -.
PATRIC; fig|1411691.4.peg.1792; -.
EchoBASE; EB3035; -.
EcoGene; EG13246; copA.
eggNOG; ENOG4105C59; Bacteria.
eggNOG; COG2217; LUCA.
HOGENOM; HOG000250397; -.
InParanoid; Q59385; -.
KO; K17686; -.
PhylomeDB; Q59385; -.
BioCyc; EcoCyc:G6260-MONOMER; -.
BioCyc; MetaCyc:G6260-MONOMER; -.
SABIO-RK; Q59385; -.
PRO; PR:Q59385; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
GO; GO:0031224; C:intrinsic component of membrane; IDA:EcoliWiki.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:EcoliWiki.
GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IDA:EcoCyc.
GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015080; F:silver ion transmembrane transporter activity; IMP:EcoCyc.
GO; GO:0071280; P:cellular response to copper ion; IEP:EcoCyc.
GO; GO:0071292; P:cellular response to silver ion; IEP:EcoCyc.
GO; GO:0060003; P:copper ion export; IDA:EcoCyc.
GO; GO:0006825; P:copper ion transport; IMP:EcoliWiki.
GO; GO:0010273; P:detoxification of copper ion; IDA:EcoCyc.
GO; GO:1902601; P:silver ion transmembrane transport; IMP:EcoCyc.
CDD; cd00371; HMA; 2.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR017969; Heavy-metal-associated_CS.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR027256; P-typ_ATPase_IB.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00403; HMA; 2.
PRINTS; PR00120; HATPASE.
SUPFAM; SSF55008; SSF55008; 2.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS01047; HMA_1; 1.
PROSITE; PS50846; HMA_2; 2.
1: Evidence at protein level;
ATP-binding; Cell inner membrane; Cell membrane; Chaperone;
Complete proteome; Copper; Copper transport; Cytoplasm;
Direct protein sequencing; Hydrolase; Ion transport; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Ribosomal frameshifting; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9868784}.
CHAIN 2 834 Copper-exporting P-type ATPase.
/FTId=PRO_0000046320.
TOPO_DOM 2 186 Cytoplasmic. {ECO:0000305}.
TRANSMEM 187 207 Helical. {ECO:0000255}.
TOPO_DOM 208 217 Periplasmic; loop 1.
{ECO:0000305|PubMed:24917681}.
TRANSMEM 218 238 Helical. {ECO:0000255}.
TOPO_DOM 239 253 Cytoplasmic. {ECO:0000305}.
TRANSMEM 254 274 Helical. {ECO:0000255}.
TOPO_DOM 275 283 Periplasmic; loop 2.
{ECO:0000305|PubMed:24917681}.
TRANSMEM 284 304 Helical. {ECO:0000255}.
TOPO_DOM 305 437 Cytoplasmic. {ECO:0000305}.
TRANSMEM 438 458 Helical. {ECO:0000255}.
TOPO_DOM 459 463 Periplasmic; loop 3. {ECO:0000305}.
TRANSMEM 464 484 Helical. {ECO:0000255}.
TOPO_DOM 485 778 Cytoplasmic. {ECO:0000305}.
TRANSMEM 779 799 Helical. {ECO:0000255}.
TOPO_DOM 800 800 Periplasmic; loop 4.
{ECO:0000305|PubMed:24917681}.
TRANSMEM 801 821 Helical. {ECO:0000255}.
TOPO_DOM 822 834 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
DOMAIN 4 65 HMA 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 100 163 HMA 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MOTIF 14 17 CXXC motif 1.
{ECO:0000305|PubMed:11500054}.
MOTIF 110 113 CXXC motif 2.
{ECO:0000305|PubMed:11500054}.
ACT_SITE 523 523 4-aspartylphosphate intermediate.
{ECO:0000305|PubMed:12351646}.
METAL 14 14 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 17 17 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 110 110 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 113 113 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 720 720 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 724 724 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
VAR_SEQ 70 834 AKPLAESSIPSEALTAVSEALPAATADDDDSQQLLLSGMSC
ASCVTRVQNALQSVPGVTQARVNLAERTALVMGSASPQDLV
QAVEKAGYGAEAIEDDAKRRERQQETAVATMKRFRWQAIVA
LAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFA
GGHFYRSAWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWP
QWFPMEARHLYYEASAMIIGLINLGHMLEARARQRSSKALE
KLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVP
VDGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDG
SVLFRASAVGSHTTLSRIIRMVRQAQSSKPEIGQLADKISA
VFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIAC
PCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTV
VFDKTGTLTEGKPQVVAVKTFADVDEAQALRLAAALEQGSS
HPLARAILDKAGDMQLPQVNGFRTLRGLGVSGEAEGHALLL
GNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGKAVA
LLAVRDPLRSDSVAALQRLHKAGYRLVMLTGDNPTTANAIA
KEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGDGINDA
PALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAI
SRATLHNMKQNLLGAFIYNSIGIPVAAGILWPFTGTLLNPV
VAGAAMALSSITVVSNANRLLRFKPKE -> G (in
isoform Soluble copper chaperone
CopA(Z)). {ECO:0000305|PubMed:28107647}.
/FTId=VSP_059176.
MUTAGEN 1 70 Missing: Slight increase in CuSO(4)-
stimulation of ATPase, no growth in
CuSO(4). Grows when this protein fragment
is provided in trans or if B.subtilis
CopZ is present.
{ECO:0000269|PubMed:25899340}.
MUTAGEN 3 113 Missing: No resistance to CuSO(4), does
not form phosphate intermediate.
{ECO:0000269|PubMed:12351646}.
MUTAGEN 7 54 Missing: Partial resistance to CuSO(4),
forms phosphate intermediate.
{ECO:0000269|PubMed:12351646}.
MUTAGEN 8 150 Missing: Loss of growth in the presence
of CuSO(4), loss of Cu efflux.
{ECO:0000269|PubMed:11500054}.
MUTAGEN 14 17 CGHC->AGHA: Wild-type growth in the
presence of CuSO(4), no change in Cu
efflux. Still forms phosphate
intermediate; when associated with 110-
A--A-113. {ECO:0000269|PubMed:11500054,
ECO:0000269|PubMed:12351646}.
MUTAGEN 14 17 CGHC->SGHS: No change in CuSO(4)-
stimulation of ATPase. When expressed as
an isolated protein fragment (residues 1-
70) does not restore growth to the 71-K--
G-834 fragment.
{ECO:0000269|PubMed:25899340}.
MUTAGEN 32 67 EQADVSITEAHVTGTASAEQLIETIKQAGYDASVSH->SRR
MCLSLKRTLPGLPVQNSRSKPSNKRVMTHLYAN:
Reduces -1 frameshifting efficiency about
2-fold in a 104 residue truncated
construct. {ECO:0000269|PubMed:28107647}.
MUTAGEN 110 113 CASC->AASA: Wild-type growth in the
presence of CuSO(4), no change in Cu
efflux. Still forms phosphate
intermediate; when associated with 14-A--
A-17. {ECO:0000269|PubMed:11500054,
ECO:0000269|PubMed:12351646}.
MUTAGEN 110 113 CASC->SASS: Loss of CuSO(4)-stimulation
of ATPase. When present in the 51-K--G-
834 fragment growth in CuSO(4) is not
restored by protein fragment 1-M--A-70.
{ECO:0000269|PubMed:25899340}.
MUTAGEN 204 204 M->A: Decreased transfer of Cu(+) to
CusF, binds 2 Cu(+).
{ECO:0000269|PubMed:24917681}.
MUTAGEN 207 210 DNMM->AAAA: First half of periplasmic
loop 1, transfers about 10% Cu(+) to
CusF. {ECO:0000269|PubMed:24917681}.
MUTAGEN 212 216 TADNR->AAANA: Second half of periplasmic
loop 1, wild-type transfer of Cu(+) to
CusF. {ECO:0000269|PubMed:24917681}.
MUTAGEN 273 277 WPQWF->APQAA: First half of periplasmic
loop 2, nearly wild-type transfer of
Cu(+) to CusF.
{ECO:0000269|PubMed:24917681}.
MUTAGEN 279 283 MEARH->AAARA: Second half of periplasmic
loop 2, wild-type transfer of Cu(+) to
CusF. {ECO:0000269|PubMed:24917681}.
MUTAGEN 287 287 E->A: Decreased transfer of Cu(+) to
CusF. {ECO:0000269|PubMed:24917681}.
MUTAGEN 479 479 C->A: Loss of copper resistance,
transport and phosphoenzyme formation.
{ECO:0000269|PubMed:12351646}.
MUTAGEN 481 481 C->A,H: Loss of copper resistance,
transport and phosphoenzyme formation.
{ECO:0000269|PubMed:12351646}.
MUTAGEN 797 802 WPFTGT->APFAGA: Periplasmic loop 4,
nearly wild-type transfer of Cu(+) to
CusF. {ECO:0000269|PubMed:24917681}.
CONFLICT 162 181 EAIEDDAKRRERQQETAVAT -> KRLKMTLNAASASKKPP
SLA (in Ref. 1; AAB02268). {ECO:0000305}.
CONFLICT 508 508 A -> R (in Ref. 1; AAB02268).
{ECO:0000305}.
CONFLICT 576 576 Q -> R (in Ref. 1; AAB02268).
{ECO:0000305}.
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


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