COPA_ARCFU
ID COPA_ARCFU Reviewed; 804 AA.
AC O29777;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable copper-exporting P-type ATPase;
DE EC=7.2.2.8 {ECO:0000269|PubMed:16495228};
DE AltName: Full=Copper-exporting P-type ATPase A;
DE AltName: Full=Cu(+)-exporting ATPase;
GN Name=copA; Synonyms=pacS; OrderedLocusNames=AF_0473;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION AS AN ATPASE, ACTIVITY REGULATION, INHIBITION BY VANADATE, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11756450; DOI=10.1074/jbc.m109964200;
RA Mandal A.K., Cheung W.D., Arguello J.M.;
RT "Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the
RT extremophile Archaeoglobus fulgidus.";
RL J. Biol. Chem. 277:7201-7208(2002).
RN [3]
RP CHARACTERIZATION, ATPASE ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751
RP AND CYS-754.
RX PubMed=12763798; DOI=10.1111/j.1749-6632.2003.tb07162.x;
RA Arguello J.M., Mandal A.K., Mana-Capelli S.;
RT "Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus
RT fulgidus.";
RL Ann. N. Y. Acad. Sci. 986:212-218(2003).
RN [4]
RP MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751 AND CYS-754.
RX PubMed=12974640; DOI=10.1021/bi034806y;
RA Mandal A.K., Arguello J.M.;
RT "Functional roles of metal binding domains of the Archaeoglobus fulgidus
RT Cu(+)-ATPase CopA.";
RL Biochemistry 42:11040-11047(2003).
RN [5]
RP REGULATION, AND INTERACTION WITH COPZ.
RX PubMed=18417453; DOI=10.1073/pnas.0711446105;
RA Gonzalez-Guerrero M., Arguello J.M.;
RT "Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly
RT transfer Cu+ to transmembrane transport sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5992-5997(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 214-326.
RX PubMed=16906753; DOI=10.1021/bi0610045;
RA Sazinsky M.H., Agarwal S., Arguello J.M., Rosenzweig A.C.;
RT "Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-
RT ATPase.";
RL Biochemistry 45:9949-9955(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 407-671, AND CATALYTIC ACTIVITY.
RX PubMed=16495228; DOI=10.1074/jbc.m510708200;
RA Sazinsky M.H., Mandal A.K., Arguello J.M., Rosenzweig A.C.;
RT "Structure of the ATP binding domain from the Archaeoglobus fulgidus Cu+-
RT ATPase.";
RL J. Biol. Chem. 281:11161-11166(2006).
CC -!- FUNCTION: Probably involved in copper and silver export.
CC {ECO:0000269|PubMed:11756450}.
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:0000269|PubMed:16495228};
CC -!- ACTIVITY REGULATION: Activated by Cu(+) and Ag(+) and inhibited by
CC vanadate. Activated by CopZ in its Cu(+)-bound form.
CC {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for ATP {ECO:0000269|PubMed:11756450,
CC ECO:0000269|PubMed:12763798};
CC Vmax=14.9 umol/h/mg enzyme with Ag(+) as substrate
CC {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
CC Vmax=3.7 umol/h/mg enzyme with Cu(+) as substrate
CC {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
CC Note=Shows higher affinity for Cu(+) compared with Ag(+).;
CC pH dependence:
CC Optimum pH is 6.1-6.5. {ECO:0000269|PubMed:11756450,
CC ECO:0000269|PubMed:12763798};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius.
CC {ECO:0000269|PubMed:11756450, ECO:0000269|PubMed:12763798};
CC -!- SUBUNIT: Interacts with CopZ probably in the CopZ Cu(+)-bound form.
CC {ECO:0000269|PubMed:18417453}.
CC -!- INTERACTION:
CC O29777; O29777: copA; NbExp=2; IntAct=EBI-9016967, EBI-9016967;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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; AE000782; AAB90763.1; -; Genomic_DNA.
DR PIR; A69309; A69309.
DR RefSeq; WP_010877980.1; NC_000917.1.
DR PDB; 2B8E; X-ray; 2.30 A; A/B/C=407-671.
DR PDB; 2HC8; X-ray; 1.65 A; A=214-325.
DR PDB; 2VOY; EM; 18.00 A; F=214-326, I=410-663, J=432-549.
DR PDB; 3A1C; X-ray; 1.85 A; A/B=398-673.
DR PDB; 3A1D; X-ray; 1.85 A; A/B=398-673.
DR PDB; 3A1E; X-ray; 1.95 A; A/B=398-673.
DR PDB; 3FRY; X-ray; 2.00 A; A/B=736-804.
DR PDB; 3J08; EM; -; A/B=93-737.
DR PDB; 3J09; EM; -; A/B=15-737.
DR PDBsum; 2B8E; -.
DR PDBsum; 2HC8; -.
DR PDBsum; 2VOY; -.
DR PDBsum; 3A1C; -.
DR PDBsum; 3A1D; -.
DR PDBsum; 3A1E; -.
DR PDBsum; 3FRY; -.
DR PDBsum; 3J08; -.
DR PDBsum; 3J09; -.
DR AlphaFoldDB; O29777; -.
DR SMR; O29777; -.
DR DIP; DIP-46021N; -.
DR STRING; 224325.AF_0473; -.
DR TCDB; 3.A.3.5.7; the p-type atpase (p-atpase) superfamily.
DR EnsemblBacteria; AAB90763; AAB90763; AF_0473.
DR GeneID; 24794013; -.
DR KEGG; afu:AF_0473; -.
DR eggNOG; arCOG01576; Archaea.
DR eggNOG; arCOG02763; Archaea.
DR HOGENOM; CLU_001771_0_3_2; -.
DR OMA; HWMLPAW; -.
DR OrthoDB; 21472at2157; -.
DR PhylomeDB; O29777; -.
DR BRENDA; 7.2.2.8; 414.
DR SABIO-RK; O29777; -.
DR EvolutionaryTrace; O29777; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; IPR006122; HMA_Cu_ion-bd.
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; 1.
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 TIGRFAMs; TIGR00003; TIGR00003; 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 3D-structure; ATP-binding; Cell membrane; Copper; Copper transport;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..804
FT /note="Probable copper-exporting P-type ATPase"
FT /id="PRO_0000350601"
FT TOPO_DOM 1..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..680
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 681..701
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 702..704
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 726..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 16..82
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 740..801
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 424
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 30
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 457..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 490..501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 618
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 622
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 751
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 754
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MUTAGEN 27
FT /note="C->A: Reduction in ATPase activity; when associated
FT with A-30."
FT /evidence="ECO:0000269|PubMed:12763798,
FT ECO:0000269|PubMed:12974640"
FT MUTAGEN 30
FT /note="C->A: Reduction in ATPase activity; when associated
FT with A-27."
FT /evidence="ECO:0000269|PubMed:12763798,
FT ECO:0000269|PubMed:12974640"
FT MUTAGEN 380
FT /note="C->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:12763798,
FT ECO:0000269|PubMed:12974640"
FT MUTAGEN 382
FT /note="C->A,S: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:12763798,
FT ECO:0000269|PubMed:12974640"
FT MUTAGEN 751
FT /note="C->A: No effect on ATPase activity; when associated
FT with A-754. Reduction in ATPase activity; when associated
FT with A-27; A-30 and A-754."
FT /evidence="ECO:0000269|PubMed:12763798,
FT ECO:0000269|PubMed:12974640"
FT MUTAGEN 754
FT /note="C->A: No effect on ATPase activity, when associated
FT with A-751. Reduction in ATPase activity; when associated
FT with A-27; A-30 and A-751."
FT /evidence="ECO:0000269|PubMed:12763798,
FT ECO:0000269|PubMed:12974640"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:2HC8"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:2HC8"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2HC8"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2HC8"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2HC8"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:2HC8"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2HC8"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:2HC8"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2HC8"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:2HC8"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2HC8"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:2HC8"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 425..429
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 435..444
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:3A1C"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 463..474
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:3A1C"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 503..508
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 515..526
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 530..536
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 539..547
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 554..563
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 576..586
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:3A1D"
FT HELIX 600..607
FT /evidence="ECO:0007829|PDB:3A1C"
FT TURN 608..610
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 613..617
FT /evidence="ECO:0007829|PDB:3A1C"
FT TURN 619..621
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 623..628
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 629..635
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 646..653
FT /evidence="ECO:0007829|PDB:3A1C"
FT HELIX 656..663
FT /evidence="ECO:0007829|PDB:3A1C"
FT STRAND 740..750
FT /evidence="ECO:0007829|PDB:3FRY"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:3FRY"
FT HELIX 755..764
FT /evidence="ECO:0007829|PDB:3FRY"
FT STRAND 768..772
FT /evidence="ECO:0007829|PDB:3FRY"
FT STRAND 774..782
FT /evidence="ECO:0007829|PDB:3FRY"
FT HELIX 783..785
FT /evidence="ECO:0007829|PDB:3FRY"
FT HELIX 786..795
FT /evidence="ECO:0007829|PDB:3FRY"
FT STRAND 799..802
FT /evidence="ECO:0007829|PDB:3FRY"
SQ 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