COPB_ARCFU
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 03-AUG-2022, entry version 142.
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 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 OMA; MALEPMG; -.
DR OrthoDB; 21472at2157; -.
DR PhylomeDB; O30085; -.
DR BRENDA; 7.2.2.9; 414.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IEA:UniProtKB-EC.
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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
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.
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
