COPA3_HELPX
ID COPA3_HELPX Reviewed; 745 AA.
AC O08462;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Copper-transporting ATPase;
DE EC=7.2.2.9;
GN Name=copA;
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=9244252; DOI=10.1128/jb.179.15.4676-4683.1997;
RA Beier D., Spohn G., Rappuoli R., Scarlato V.;
RT "Identification and characterization of an operon of Helicobacter pylori
RT that is involved in motility and stress adaptation.";
RL J. Bacteriol. 179:4676-4683(1997).
CC -!- FUNCTION: Probably involved in copper export.
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 -!- 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; U97567; AAB66380.1; -; Genomic_DNA.
DR AlphaFoldDB; O08462; -.
DR SMR; O08462; -.
DR STRING; 1345592.CBOM010000004_gene528; -.
DR eggNOG; COG2217; Bacteria.
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 CDD; cd00371; HMA; 1.
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; 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; 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.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..745
FT /note="Copper-transporting ATPase"
FT /id="PRO_0000046173"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..379
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 706..716
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..67
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 435
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 15
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 631
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 635
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 745 AA; 81845 MW; 604CA6DC74B13480 CRC64;
MKESFYIEGM TCTACSSGIE RSLGRKSFVK KIEVSLLNKS ANIEFNENET NLDEIFKLIE
KLGYSPKKTL AEEKKEFFSP NVKLALAVIF TLFVVYLSMG AMLSPSLLPE SLLAINNHSN
FLNACLQLIG ALIVMHLGRD FYIQGFKALW HRQPNMSSLI AIGTSAALIS SLWQLYLVYT
NHYTDQWSYG HYYFESVCVI LMFVMVGKRI ENVSKDKALD AMQALMKNAP KTALKMQNNQ
QIEVLVDSIV VGDILKVLPG SAIAVDGEII EGEGELDESM LSGEALPVYK KVGDKVFSGT
LNSHTSFLMK ATQNNKNSTL SQIIEMIHNA QSSKAEISRL ADKVSSVFVP SVIAIAILAF
VVWLIIAPKP DFWWNFGIAL EVFVSVLVIS CPCALGLATP MSILVANQKA SSLGLFFKDA
KSLEKARLVN TIVFDKTGTL TNGKPVVKSV HSKIELLELL SLAGSIEKSS EHVIAKGIVE
YAKERNAPLK EMSEVKVKTG FGISAKTDYQ GIKEIIKVGN SEFFNPINTL EIKENGILVF
VGRAISEKED ELLGVFVLED LPKKGVKEHI AQIKNLGINT FLLSGDNREN VKKCALELGI
DGYISNAKPQ DKLNKIKELK EQGQIVMMVG DGLNDAPSLA MNDVAVVMAK GSDVSVQAAD
IVSFNNDIKS VYSAIKLSQA TIKNIKENLF WAFCYNSVFI PLACGVLYKA NIMLSPAIAG
LAMSLSSVSV VLNSQRLRNF KIKDH
