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Probable copper-exporting P-type ATPase (EC 3.6.3.54) (Copper-exporting P-type ATPase A) (Cu( )-exporting ATPase)

 COPA_ARCFU              Reviewed;         804 AA.
O29777;
23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 133.
RecName: Full=Probable copper-exporting P-type ATPase;
EC=3.6.3.54;
AltName: Full=Copper-exporting P-type ATPase A;
AltName: Full=Cu(+)-exporting ATPase;
Name=copA; Synonyms=pacS; OrderedLocusNames=AF_0473;
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
9628 / NBRC 100126).
Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
Archaeoglobaceae; Archaeoglobus.
NCBI_TaxID=224325;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
PubMed=9389475; DOI=10.1038/37052;
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
Woese C.R., Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-
reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).
[2]
FUNCTION AS AN ATPASE, ENZYME REGULATION, INHIBITION BY VANADATE, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11756450; DOI=10.1074/jbc.M109964200;
Mandal A.K., Cheung W.D., Arguello J.M.;
"Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the
extremophile Archaeoglobus fulgidus.";
J. Biol. Chem. 277:7201-7208(2002).
[3]
CHARACTERIZATION, ATPASE ACTIVITY, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-27; CYS-30;
CYS-380; CYS-382; CYS-751 AND CYS-754.
PubMed=12763798; DOI=10.1111/j.1749-6632.2003.tb07162.x;
Arguello J.M., Mandal A.K., Mana-Capelli S.;
"Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus
fulgidus.";
Ann. N. Y. Acad. Sci. 986:212-218(2003).
[4]
MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751 AND CYS-754.
PubMed=12974640; DOI=10.1021/bi034806y;
Mandal A.K., Arguello J.M.;
"Functional roles of metal binding domains of the Archaeoglobus
fulgidus Cu(+)-ATPase CopA.";
Biochemistry 42:11040-11047(2003).
[5]
REGULATION, AND INTERACTION WITH COPZ.
PubMed=18417453; DOI=10.1073/pnas.0711446105;
Gonzalez-Guerrero M., Arguello J.M.;
"Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones
directly transfer Cu+ to transmembrane transport sites.";
Proc. Natl. Acad. Sci. U.S.A. 105:5992-5997(2008).
[6]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 214-326.
PubMed=16906753; DOI=10.1021/bi0610045;
Sazinsky M.H., Agarwal S., Arguello J.M., Rosenzweig A.C.;
"Structure of the actuator domain from the Archaeoglobus fulgidus
Cu(+)-ATPase.";
Biochemistry 45:9949-9955(2006).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 407-671, AND CATALYTIC
ACTIVITY.
PubMed=16495228; DOI=10.1074/jbc.M510708200;
Sazinsky M.H., Mandal A.K., Arguello J.M., Rosenzweig A.C.;
"Structure of the ATP binding domain from the Archaeoglobus fulgidus
Cu+-ATPase.";
J. Biol. Chem. 281:11161-11166(2006).
-!- FUNCTION: Probably involved in copper and silver export.
{ECO:0000269|PubMed:11756450}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate
+ Cu(+)(Side 2). {ECO:0000269|PubMed:16495228}.
-!- ENZYME REGULATION: Activated by Cu(+) and Ag(+) and inhibited by
vanadate. Activated by CopZ in its Cu(+)-bound form.
{ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.25 mM for ATP {ECO:0000269|PubMed:11756450,
ECO:0000269|PubMed:12763798};
Vmax=14.9 umol/h/mg enzyme with Ag(+) as substrate
{ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
Vmax=3.7 umol/h/mg enzyme with Cu(+) as substrate
{ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
Note=Shows higher affinity for Cu(+) compared with Ag(+).;
pH dependence:
Optimum pH is 6.1-6.5. {ECO:0000269|PubMed:11756450,
ECO:0000269|PubMed:12763798};
Temperature dependence:
Optimum temperature is 75 degrees Celsius.
{ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
-!- SUBUNIT: Interacts with CopZ probably in the CopZ Cu(+)-bound
form. {ECO:0000269|PubMed:18417453}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-9016967, EBI-9016967;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE000782; AAB90763.1; -; Genomic_DNA.
PIR; A69309; A69309.
RefSeq; WP_010877980.1; NC_000917.1.
PDB; 2B8E; X-ray; 2.30 A; A/B/C=407-671.
PDB; 2HC8; X-ray; 1.65 A; A=214-325.
PDB; 2VOY; EM; 18.00 A; F=214-326, I=410-663, J=432-549.
PDB; 3A1C; X-ray; 1.85 A; A/B=398-673.
PDB; 3A1D; X-ray; 1.85 A; A/B=398-673.
PDB; 3A1E; X-ray; 1.95 A; A/B=398-673.
PDB; 3FRY; X-ray; 2.00 A; A/B=736-804.
PDB; 3J08; EM; -; A/B=93-737.
PDB; 3J09; EM; -; A/B=15-737.
PDBsum; 2B8E; -.
PDBsum; 2HC8; -.
PDBsum; 2VOY; -.
PDBsum; 3A1C; -.
PDBsum; 3A1D; -.
PDBsum; 3A1E; -.
PDBsum; 3FRY; -.
PDBsum; 3J08; -.
PDBsum; 3J09; -.
ProteinModelPortal; O29777; -.
SMR; O29777; -.
DIP; DIP-46021N; -.
STRING; 224325.AF0473; -.
TCDB; 3.A.3.5.7; the p-type atpase (p-atpase) superfamily.
PRIDE; O29777; -.
EnsemblBacteria; AAB90763; AAB90763; AF_0473.
GeneID; 24794013; -.
KEGG; afu:AF_0473; -.
eggNOG; arCOG01576; Archaea.
eggNOG; COG2217; LUCA.
KO; K17686; -.
OMA; HWMLPAW; -.
OrthoDB; POG093Z00O0; -.
BRENDA; 3.6.3.54; 414.
SABIO-RK; O29777; -.
EvolutionaryTrace; O29777; -.
Proteomes; UP000002199; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
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; IPR006122; HMA_Cu_ion-bd.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR027256; P-typ_ATPase_IB.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00403; HMA; 2.
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.
TIGRFAMs; TIGR00003; TIGR00003; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS01047; HMA_1; 1.
PROSITE; PS50846; HMA_2; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane; Complete proteome; Copper;
Copper transport; Hydrolase; Ion transport; Magnesium; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 804 Probable copper-exporting P-type ATPase.
/FTId=PRO_0000350601.
TOPO_DOM 1 101 Cytoplasmic. {ECO:0000255}.
TRANSMEM 102 122 Helical. {ECO:0000255}.
TOPO_DOM 123 128 Extracellular. {ECO:0000255}.
TRANSMEM 129 149 Helical. {ECO:0000255}.
TOPO_DOM 150 159 Cytoplasmic. {ECO:0000255}.
TRANSMEM 160 180 Helical. {ECO:0000255}.
TOPO_DOM 181 186 Extracellular. {ECO:0000255}.
TRANSMEM 187 204 Helical. {ECO:0000255}.
TOPO_DOM 205 339 Cytoplasmic. {ECO:0000255}.
TRANSMEM 340 360 Helical. {ECO:0000255}.
TOPO_DOM 361 364 Extracellular. {ECO:0000255}.
TRANSMEM 365 385 Helical. {ECO:0000255}.
TOPO_DOM 386 680 Cytoplasmic. {ECO:0000255}.
TRANSMEM 681 701 Helical. {ECO:0000255}.
TOPO_DOM 702 704 Extracellular. {ECO:0000255}.
TRANSMEM 705 725 Helical. {ECO:0000255}.
TOPO_DOM 726 804 Cytoplasmic. {ECO:0000255}.
DOMAIN 17 83 HMA 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 741 802 HMA 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
NP_BIND 457 462 ATP. {ECO:0000255}.
NP_BIND 490 501 ATP. {ECO:0000255}.
ACT_SITE 424 424 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 27 27 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 30 30 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 618 618 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 622 622 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 751 751 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 754 754 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MUTAGEN 27 27 C->A: Reduction in ATPase activity; when
associated with A-30.
{ECO:0000269|PubMed:12763798,
ECO:0000269|PubMed:12974640}.
MUTAGEN 30 30 C->A: Reduction in ATPase activity; when
associated with A-27.
{ECO:0000269|PubMed:12763798,
ECO:0000269|PubMed:12974640}.
MUTAGEN 380 380 C->A: Abolishes activity.
{ECO:0000269|PubMed:12763798,
ECO:0000269|PubMed:12974640}.
MUTAGEN 382 382 C->A,S: Abolishes activity.
{ECO:0000269|PubMed:12763798,
ECO:0000269|PubMed:12974640}.
MUTAGEN 751 751 C->A: No effect on ATPase activity; when
associated with A-754. Reduction in
ATPase activity; when associated with A-
27; A-30 and A-754.
{ECO:0000269|PubMed:12763798,
ECO:0000269|PubMed:12974640}.
MUTAGEN 754 754 C->A: No effect on ATPase activity, when
associated with A-751. Reduction in
ATPase activity; when associated with A-
27; A-30 and A-751.
{ECO:0000269|PubMed:12763798,
ECO:0000269|PubMed:12974640}.
HELIX 215 222 {ECO:0000244|PDB:2HC8}.
STRAND 225 231 {ECO:0000244|PDB:2HC8}.
STRAND 234 239 {ECO:0000244|PDB:2HC8}.
HELIX 240 242 {ECO:0000244|PDB:2HC8}.
STRAND 248 251 {ECO:0000244|PDB:2HC8}.
STRAND 259 265 {ECO:0000244|PDB:2HC8}.
STRAND 268 271 {ECO:0000244|PDB:2HC8}.
HELIX 273 276 {ECO:0000244|PDB:2HC8}.
STRAND 282 284 {ECO:0000244|PDB:2HC8}.
STRAND 301 307 {ECO:0000244|PDB:2HC8}.
HELIX 309 311 {ECO:0000244|PDB:2HC8}.
HELIX 313 325 {ECO:0000244|PDB:2HC8}.
STRAND 404 406 {ECO:0000244|PDB:3A1C}.
HELIX 411 417 {ECO:0000244|PDB:3A1C}.
STRAND 420 424 {ECO:0000244|PDB:3A1C}.
HELIX 425 429 {ECO:0000244|PDB:3A1C}.
STRAND 435 444 {ECO:0000244|PDB:3A1C}.
HELIX 446 456 {ECO:0000244|PDB:3A1C}.
TURN 457 459 {ECO:0000244|PDB:3A1C}.
HELIX 463 474 {ECO:0000244|PDB:3A1C}.
STRAND 485 488 {ECO:0000244|PDB:3A1C}.
TURN 489 491 {ECO:0000244|PDB:3A1C}.
STRAND 492 495 {ECO:0000244|PDB:3A1C}.
STRAND 498 501 {ECO:0000244|PDB:3A1C}.
HELIX 503 508 {ECO:0000244|PDB:3A1C}.
HELIX 515 526 {ECO:0000244|PDB:3A1C}.
STRAND 530 536 {ECO:0000244|PDB:3A1C}.
STRAND 539 547 {ECO:0000244|PDB:3A1C}.
HELIX 554 563 {ECO:0000244|PDB:3A1C}.
STRAND 567 571 {ECO:0000244|PDB:3A1C}.
HELIX 576 586 {ECO:0000244|PDB:3A1C}.
STRAND 589 592 {ECO:0000244|PDB:3A1C}.
HELIX 597 599 {ECO:0000244|PDB:3A1D}.
HELIX 600 607 {ECO:0000244|PDB:3A1C}.
TURN 608 610 {ECO:0000244|PDB:3A1C}.
STRAND 613 617 {ECO:0000244|PDB:3A1C}.
TURN 619 621 {ECO:0000244|PDB:3A1C}.
HELIX 623 628 {ECO:0000244|PDB:3A1C}.
STRAND 629 635 {ECO:0000244|PDB:3A1C}.
STRAND 646 653 {ECO:0000244|PDB:3A1C}.
HELIX 656 663 {ECO:0000244|PDB:3A1C}.
STRAND 740 750 {ECO:0000244|PDB:3FRY}.
HELIX 752 754 {ECO:0000244|PDB:3FRY}.
HELIX 755 764 {ECO:0000244|PDB:3FRY}.
STRAND 768 772 {ECO:0000244|PDB:3FRY}.
STRAND 774 782 {ECO:0000244|PDB:3FRY}.
HELIX 783 785 {ECO:0000244|PDB:3FRY}.
HELIX 786 795 {ECO:0000244|PDB:3FRY}.
STRAND 799 802 {ECO:0000244|PDB:3FRY}.
SEQUENCE 804 AA; 86432 MW; 610EB948C1D6B16F CRC64;
MVKDTYISSA SKTPPMERTV RVTGMTCAMC VKSIETAVGS LEGVEEVRVN LATETAFIRF
DEKRIDFETI KRVIEDLGYG VVDEQAAVSA EVEHLSRMKR KLYVAAFAGV LLLFLAHFIS
LPYEDFVQLL IALPAIFYSG SSIFKAAFSA LRRRTLNMDV MYSMGVGAAF LASVLSTAGV
LPREYSFYET SVLLLAFLLL GRTLEARAKS RTGEAIKKLV GLQAKTAVVI RDGKEIAVPV
EEVAVGDIVI VRPGEKIPVD GVVVEGESYV DESMISGEPV PVLKSKGDEV FGATINNTGV
LKIRATRVGG ETLLAQIVKL VEDAMGSKPP IQRLADKVVA YFIPTVLLVA ISAFIYWYFI
AHAPLLFAFT TLIAVLVVAC PCAFGLATPT ALTVGMGKGA ELGILIKNAD ALEVAEKVTA
VIFDKTGTLT KGKPEVTDLV PLNGDERELL RLAAIAERRS EHPIAEAIVK KALEHGIELG
EPEKVEVIAG EGVVADGILV GNKRLMEDFG VAVSNEVELA LEKLEREAKT AVIVARNGRV
EGIIAVSDTL KESAKPAVQE LKRMGIKVGM ITGDNWRSAE AISRELNLDL VIAEVLPHQK
SEEVKKLQAK EVVAFVGDGI NDAPALAQAD LGIAVGSGSD VAVESGDIVL IRDDLRDVVA
AIQLSRKTMS KIKQNIFWAL IYNVILIPAA AGLLYPIFGV VFRPEFAGLA MAMSSVSVVA
NSLLLRNYVP PIRRGGDSVE KIVLELSGLS CHHCVARVKK ALEEAGAKVE KVDLNEAVVA
GNKEDVDKYI KAVEAAGYQA KLRS


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