ID   COPB_ARCFU              Reviewed;         690 AA.
AC   O30085;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Copper-exporting P-type ATPase B;
DE            EC=7.2.2.9;
GN   Name=copB; OrderedLocusNames=AF_0152;
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   CHARACTERIZATION, ATPASE ACTIVITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
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   [3]
RP   FUNCTION AS A COPPER ATPASE, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=12876283; DOI=10.1074/jbc.m306907200;
RA   Mana-Capelli S., Mandal A.K., Arguello J.M.;
RT   "Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role
RT   of its histidine-rich-N-terminal metal binding domain.";
RL   J. Biol. Chem. 278:40534-40541(2003).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 372-636 OF APOENZYME AND IN
RP   COMPLEX WITH PHOSPHATE, FUNCTION, AND ACTIVE SITE.
RX   PubMed=22663904; DOI=10.1042/bsr20120048;
RA   Jayakanthan S., Roberts S.A., Weichsel A., Arguello J.M., McEvoy M.M.;
RT   "Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding
RT   domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to
RT   the catalytic cycle.";
RL   Biosci. Rep. 32:443-453(2012).
CC   -!- FUNCTION: Involved in copper export. {ECO:0000269|PubMed:12876283,
CC       ECO:0000269|PubMed:22663904}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.9;
CC   -!- ACTIVITY REGULATION: Activated by Cu(2+) and to a lesser extent by
CC       Ag(+) and Cu(+). {ECO:0000269|PubMed:12763798,
CC       ECO:0000269|PubMed:12876283}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.7. {ECO:0000269|PubMed:12763798,
CC         ECO:0000269|PubMed:12876283};
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius.
CC         {ECO:0000269|PubMed:12763798, ECO:0000269|PubMed:12876283};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The histidine-N-terminal metal-binding domain (His-N-MBD) seems
CC       to have a regulatory role affecting the metal transport rate by
CC       controlling the metal release/dephosphorylation rates.
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; AAB91079.1; -; Genomic_DNA.
DR   PIR; H69268; H69268.
DR   RefSeq; WP_010877664.1; NC_000917.1.
DR   PDB; 3SKX; X-ray; 1.59 A; A=372-636.
DR   PDB; 3SKY; X-ray; 2.10 A; A=372-636.
DR   PDBsum; 3SKX; -.
DR   PDBsum; 3SKY; -.
DR   AlphaFoldDB; O30085; -.
DR   SMR; O30085; -.
DR   STRING; 224325.AF_0152; -.
DR   TCDB; 3.A.3.5.10; the p-type atpase (p-atpase) superfamily.
DR   PaxDb; 224325-AF_0152; -.
DR   EnsemblBacteria; AAB91079; AAB91079; AF_0152.
DR   GeneID; 24793702; -.
DR   KEGG; afu:AF_0152; -.
DR   eggNOG; arCOG01576; Archaea.
DR   HOGENOM; CLU_001771_11_2_2; -.
DR   OrthoDB; 8588at2157; -.
DR   PhylomeDB; O30085; -.
DR   BRENDA; 7.2.2.9; 414.
DR   Proteomes; UP000002199; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043682; F:P-type divalent copper transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd07552; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
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; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..690
FT                   /note="Copper-exporting P-type ATPase B"
FT                   /id="PRO_0000350609"
FT   TOPO_DOM        1..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..151
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..303
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..336
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..640
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        641..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        662..663
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        664..684
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        685..690
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          23..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        389
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000269|PubMed:22663904"
FT   BINDING         390..391
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT   BINDING         537..538
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT   BINDING         565
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000269|PubMed:22663904"
FT   BINDING         583
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         587
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   HELIX           376..379
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           380..382
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          385..389
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           390..394
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          395..409
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           411..422
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           428..439
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          448..453
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   TURN            454..456
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          457..462
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          465..470
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           472..477
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           486..490
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   TURN            491..493
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          495..501
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          504..515
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           519..528
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          532..536
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           541..551
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          554..557
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           562..564
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           565..573
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          578..582
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   TURN            584..587
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           588..593
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          594..599
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          604..606
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   STRAND          610..614
FT                   /evidence="ECO:0007829|PDB:3SKX"
FT   HELIX           622..631
FT                   /evidence="ECO:0007829|PDB:3SKX"
SQ   SEQUENCE   690 AA;  75383 MW;  AA063EF54B4F5EA2 CRC64;
     MHEHDSHGEA AHSNSEDMQM IHQHHEHHGH EEEHSAHHEK MKHSADHGDH HRMMMEDFKK
     RFYVSTLLTI PILILSPAIQ TFLGFRVEFA GSLYILFLLS SAVYFYGGYP FLKGIFDELR
     RRQPGMMTLI AVAISVAYFY SSAVVFGLKG KFFFWELATL IDIMLLGHYI EMRSVLGASR
     ALEELVKIMP SEAHLLKDGE IVEVKVENLK PGDKVLVKPG EKIPVDGIVV EGESFVNEAM
     LTGESKPVAK KPGDTVIGGA INGEGSLVVE VEKTGKDTYL NQVIELVRQA QESKSRTQDL
     ANRAALLLTV IALTVGSVTL AIWLAYIADF AFAIERAVTV MVITCPHALG LAIPLVVAVS
     TSLAAKSGLL IRDRQAFERA KDLQAVIFDK TGTLTEGRFG VTDIVGFNHS EDELLQIAAS
     LEARSEHPIA AAIVEEAEKR GFGLTEVEEF RAIPGKGVEG IVNGRRYMVV SPGYIRELGI
     KTDESVEKLK QQGKTVVFIL KNGEVSGVIA LADRIRPESR EAISKLKAIG IKCMMLTGDN
     RFVAKWVAEE LGLDDYFAEV LPHEKAEKVK EVQQKYVTAM VGDGVNDAPA LAQADVGIAI
     GAGTDVAVET ADIVLVRNDP RDVAAIVELS RKTYSKMKQN LLWATGYNAF AIPLAAGVLY
     SAGILLSPAV GAILMSLSTV IVAINARLLR
//