COPA1_HELPX
ID COPA1_HELPX Reviewed; 745 AA.
AC P77871;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802;
RX PubMed=7752900; DOI=10.1111/j.1365-2958.1995.tb02224.x;
RA Ge Z., Hiratsuka K., Taylor D.E.;
RT "Nucleotide sequence and mutational analysis indicate that two Helicobacter
RT pylori genes encode a P-type ATPase and a cation-binding protein associated
RT with copper transport.";
RL Mol. Microbiol. 15:97-106(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802;
RX PubMed=8961555; DOI=10.1111/j.1574-6968.1996.tb08575.x;
RA Ge Z., Taylor D.E.;
RT "Helicobacter pylori genes hpcopA and hpcopP constitute a cop operon
RT involved in copper export.";
RL FEMS Microbiol. Lett. 145:181-188(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67320.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L33259; AAB67320.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; P77871; -.
DR SMR; P77871; -.
DR PRIDE; P77871; -.
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; SSF81660; SSF81660; 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_0000046171"
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; 82029 MW; 043168CF0622245B CRC64;
MKESFYIEGM TCTACSSGIE RSLGRKSFVK KIEVNLLNKS ANIEFNENET NLDEIFKLIE
KLGYSPKKTL AEEKKEFFSP NVKLALAVIF TLFVVYLSMG AMLSPSLLPK SLLAIDNHSN
FLNACLQLIG TLIVMHWGRD FYIQGFKALW HRQPNMSSLI AIGTSAALIS SLWQLYLVYT
DHYTDQWSYG HYYFESVCVI LMFVMVGKRI ENVSKDKALD AMQALMKNAP KTALKIQNDQ
QIEVLVDSIV VGDILKVLPG TLIAVDGEII EGEGELDESM LSGEALPVYK KVGDKVFSGT
FNSHTSFLMK ATQNNKNSTL SQIVEMIHNA QSSKAEISRL ADKVSSVFVP SVIAIAILAF
VVWLIIAPKP DFWWNFGIAL EVFVSVLVIS CPCALGLATL MSILVANQKA SSLGLFFKDA
KSLEKARLVN TIVFDKTGTL TNGKPVVKSV HSKIELLELL SLANSIEKSS EHVIAKGIVE
YAKEHNAPLK EMSEVKVKTG FGISAKTDYQ GTKEIIKVGN SEFFNPINTL EIQENGILVL
VGRAINEKED ELLGAFVLED LPKKGVKEHV AQIKNLGINT FLLSGDNREN VKKCALELGI
DGYISNAKPQ DKLNKIKELK EKGRIVMMVG DGLNDAPSLA MSDVAVVMAK GSDVSVQAAD
IVSFNNDIKS VYSAIKLSQA TIKNIKENLF WAFCYNSVFI PLACGVLYKA NIMLSPAIAG
LAMSLSSVSV VLNSQRLRNF KIKDH
