HMCT_HELPJ
ID HMCT_HELPJ Reviewed; 686 AA.
AC Q9ZL53;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cadmium, zinc and cobalt-transporting ATPase;
DE EC=7.2.2.12;
DE EC=7.2.2.21;
GN Name=cadA; OrderedLocusNames=jhp_0727;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: Couples the hydrolysis of ATP with the transport of cadmium,
CC zinc and cobalt out of the cell.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.21;
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; AE001439; AAD06308.1; -; Genomic_DNA.
DR PIR; E71895; E71895.
DR RefSeq; WP_001158764.1; NC_000921.1.
DR AlphaFoldDB; Q9ZL53; -.
DR SMR; Q9ZL53; -.
DR STRING; 85963.jhp_0727; -.
DR EnsemblBacteria; AAD06308; AAD06308; jhp_0727.
DR KEGG; hpj:jhp_0727; -.
DR eggNOG; COG2217; Bacteria.
DR OMA; AQVVIMN; -.
DR Proteomes; UP000000804; 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:0008551; F:P-type cadmium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0016463; F:P-type zinc 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 PRINTS; PR00941; CDATPASE.
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; Cadmium; Cell membrane; Cobalt; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Translocase;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..686
FT /note="Cadmium, zinc and cobalt-transporting ATPase"
FT /id="PRO_0000046177"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 73..92
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 93..102
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 103..124
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 125..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 132..151
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 152..154
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 175..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 309..327
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 328..332
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 333..350
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 351..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 636..657
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 658..665
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 666..681
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 682..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1..62
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 388
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 11
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 14
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 14
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 583
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 587
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 686 AA; 74837 MW; 01E39A3B057476E2 CRC64;
MQEYHIHNLD CPDCAAKLER DLNKLDYVKK AQINFSTSKL FLDTSDFEKV KAFIKQNEPH
LSLSFKEAAE KPLSFTPLIA TIAVFLGAIL ILHLEPSPFI EKAVFVVLAL VYLISGKDVI
LGAFRGLRKG QFFDENALML IATIAAFCVG AYEESVSIMV FYSAGEFLQI LAIARSKKSL
KALVDVAPNL AYLKKGDTLV SVAPEDLRIN DIVVVKVGEK VPVDGVVIKG ESLLDERALS
GESMPVNVSE RSKVLGGSLN LKAVLEIQVE KLYKDSSIAK VVDLVQQATN EKSETEKFIT
KFSRYYTPSV LFIALMIAVL PPLFSMGSFD EWIYRGLVAL MVSCPCALVI SVPLGYFGGV
GAASRKGILM KGVHVLEVLT QTKSIAFDKT GTLTKGVFKV VDIVPQNGHS KEEVLHYASC
SQLLSTHPIA LSIQKACEEM LKDDKHQHDI KNYEELSGMG VKAQCHTDLI IAGNEKMLDQ
FHIAHSPSPE NGTIVHVAFN QTYIGYIVIS DEIKDDAIEC LRDLKAQGIE NFCILSGDRK
SATESIARTL GCEYHASLLP EEKTSVFKTF KERYKAPAIF VGDGINDAPT LASADVGIGM
GKGSELSKQS ADIVITNDSL SSLVKVLAIA KKTKSIIWQN ILFALGIKAV FIVLGLMGVA
SLWEAVFGDV GVTLLALANS MRTMRA
