COPA_HELPY
ID COPA_HELPY Reviewed; 745 AA.
AC P55989;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Copper-transporting ATPase;
DE EC=7.2.2.9;
GN Name=copA; OrderedLocusNames=HP_1072;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(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; AE000511; AAD08117.1; -; Genomic_DNA.
DR PIR; H64653; H64653.
DR RefSeq; NP_207863.1; NC_000915.1.
DR RefSeq; WP_000664941.1; NC_018939.1.
DR AlphaFoldDB; P55989; -.
DR SMR; P55989; -.
DR DIP; DIP-3096N; -.
DR IntAct; P55989; 14.
DR MINT; P55989; -.
DR STRING; 85962.C694_05540; -.
DR PaxDb; P55989; -.
DR EnsemblBacteria; AAD08117; AAD08117; HP_1072.
DR KEGG; hpy:HP_1072; -.
DR PATRIC; fig|85962.47.peg.1151; -.
DR eggNOG; COG2217; Bacteria.
DR OMA; ACGMNMV; -.
DR PhylomeDB; P55989; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
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 Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..745
FT /note="Copper-transporting ATPase"
FT /id="PRO_0000046170"
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; 81853 MW; 855C10A737C072C9 CRC64;
MKESFYIEGM TCTACSSGIE RSLGRKSFVK KIEVSLLNKS ANIEFDENQT NLDEIFKLIE
KLGYSPKKAL TKEKKEFFSP NVKLALAVIF TLFVVYLSMG AMLSPSLLPE SLLAIDNHSN
FLNACLQLIG ALIVMHLGRD FYIQGFKALW HRQPNMSSLI AIGTSAALIS SLWQLYLVYT
NHYTDQWSYG HYYFESVCVI LMFVMVGKRI ENVSKDKALD AMQALMKNAP KTALKMQNNQ
QIEVLVDSIV VGDILKVLPG SAIAVDGEII EGEGELDESM LSGEALPVYK KVGDKVFSGT
FNSHTSFLMK ATQNNKNSTL SQIIEMIYNA QSSKAEISRL ADKVSSVFVP SVIAISILAF
VVWLIIAPKP DFWWNFGIAL EVFVSVLVIS CPCALGLATP MSILVANQKA SSLGLFFKDA
KSLEKARLVN TIVFDKTGTL TNGKPVVKSV HSKIELLELL SLALSIEKSS EHVIAKGIVE
YAKEHNAPLK EMSGVKVKTG FGISAKTDYQ GTKEIIKVGN SEFFNPINTL EIKENGILVF
VGRAISEKED ELLGAFVLED LPKKGVKEHI AQIKNLGINT FLLSGDNREN VQKCAFELGI
DGYISNAKPQ DKLNKIKELK EKGQIVMMVG DGLNDAPSLA MSDVAVVMAK GSDVSVQAAD
IVSFNNDIKS VYSAIKLSQA TIKNIKENLF WAFCYNSVFI PLACGVLYKA NLMLSPAIAG
LAMSLSSVSV VLNSQRLRNF KIKDH
