HMCT_HELPY
ID HMCT_HELPY Reviewed; 686 AA.
AC Q59465;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 155.
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=HP_0791;
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 [GENOMIC DNA].
RC STRAIN=69A;
RX PubMed=8550601; DOI=10.1074/jbc.271.1.446;
RA Melchers K., Weitzenegger T., Buhmann A., Steinhilber W., Sachs G.,
RA Schaefer K.P.;
RT "Cloning and membrane topology of a P type ATPase from Helicobacter
RT pylori.";
RL J. Biol. Chem. 271:446-457(1996).
RN [2]
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).
RN [3]
RP TOPOLOGY.
RC STRAIN=69A;
RX PubMed=10417643; DOI=10.1046/j.1365-2958.1999.01496.x;
RA Herrmann L., Schwan D., Garner R., Mobley H.L., Haas R., Schaefer K.P.,
RA Melchers K.;
RT "Helicobacter pylori cadA encodes an essential Cd(II)-Zn(II)-Co(II)
RT resistance factor influencing urease activity.";
RL Mol. Microbiol. 33:524-536(1999).
RN [4]
RP SUBSTRATE SPECIFICITY.
RC STRAIN=69A;
RX PubMed=10577484; DOI=10.1016/s0923-2508(99)00106-0;
RA Melchers K., Schuhmacher A., Buhmann A., Weitzenegger T., Belin D.,
RA Grau S., Ehrmann M.;
RT "Membrane topology of CadA homologous P-type ATPase of Helicobacter pylori
RT as determined by expression of phoA fusions in Escherichia coli and the
RT positive inside rule.";
RL Res. Microbiol. 150:507-520(1999).
CC -!- FUNCTION: Couples the hydrolysis of ATP with the transport of cadmium,
CC zinc and cobalt out of the cell. This ion efflux may influence the
CC activity of urease, which is essential for the survival of the
CC bacterium in the gastric environment.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L46864; AAA93043.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07839.1; -; Genomic_DNA.
DR PIR; G64618; G64618.
DR RefSeq; NP_207584.1; NC_000915.1.
DR RefSeq; WP_001158808.1; NC_018939.1.
DR AlphaFoldDB; Q59465; -.
DR SMR; Q59465; -.
DR DIP; DIP-3082N; -.
DR IntAct; Q59465; 3.
DR MINT; Q59465; -.
DR STRING; 85962.C694_04055; -.
DR TCDB; 3.A.3.6.3; the p-type atpase (p-atpase) superfamily.
DR PaxDb; Q59465; -.
DR DNASU; 899347; -.
DR EnsemblBacteria; AAD07839; AAD07839; HP_0791.
DR KEGG; hpy:HP_0791; -.
DR PATRIC; fig|85962.47.peg.843; -.
DR eggNOG; COG2217; Bacteria.
DR OMA; AQVVIMN; -.
DR PhylomeDB; Q59465; -.
DR Proteomes; UP000000429; 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:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
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 GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030001; P:metal ion transport; IMP:CACAO.
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 1: Evidence at protein level;
KW ATP-binding; Cadmium; Cell membrane; Cobalt; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..686
FT /note="Cadmium, zinc and cobalt-transporting ATPase"
FT /id="PRO_0000046176"
FT TOPO_DOM 1..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10417643"
FT TRANSMEM 73..92
FT /note="Helical; Name=1"
FT TOPO_DOM 93..102
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10417643"
FT TRANSMEM 103..124
FT /note="Helical; Name=2"
FT TOPO_DOM 125..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10417643"
FT TRANSMEM 132..151
FT /note="Helical; Name=3"
FT TOPO_DOM 152..154
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10417643"
FT TRANSMEM 155..174
FT /note="Helical; Name=4"
FT TOPO_DOM 175..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10417643"
FT TRANSMEM 309..327
FT /note="Helical; Name=5"
FT TOPO_DOM 328..332
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10417643"
FT TRANSMEM 333..350
FT /note="Helical; Name=6"
FT TOPO_DOM 351..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10417643"
FT TRANSMEM 636..657
FT /note="Helical; Name=7"
FT TOPO_DOM 658..665
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10417643"
FT TRANSMEM 666..681
FT /note="Helical; Name=8"
FT TOPO_DOM 682..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10417643"
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"
FT VARIANT 24
FT /note="E -> K (in strain: 69A)"
FT VARIANT 39
FT /note="K -> R (in strain: 69A)"
FT VARIANT 69
FT /note="T -> A (in strain: 69A)"
FT VARIANT 80
FT /note="I -> V (in strain: 69A)"
FT VARIANT 83
FT /note="M -> A (in strain: 69A)"
FT VARIANT 148
FT /note="F -> C (in strain: 69A)"
FT VARIANT 173..174
FT /note="VS -> IA (in strain: 69A)"
FT VARIANT 198
FT /note="E -> A (in strain: 69A)"
FT VARIANT 209
FT /note="V -> I (in strain: 69A)"
FT VARIANT 228
FT /note="V -> I (in strain: 69A)"
FT VARIANT 251
FT /note="N -> R (in strain: 69A)"
FT VARIANT 435
FT /note="K -> E (in strain: 69A)"
FT VARIANT 456
FT /note="V -> L (in strain: 69A)"
FT VARIANT 504
FT /note="V -> I (in strain: 69A)"
FT VARIANT 526
FT /note="V -> A (in strain: 69A)"
FT VARIANT 555
FT /note="H -> Y (in strain: 69A)"
SQ SEQUENCE 686 AA; 75012 MW; 8777A49D80397E19 CRC64;
MQEYHIHNLD CPDCASKLER DLNELDYVKK AQINFSTSKL FLDTSDFEKV KAFIKQNEPH
LSLSFKEATE KPLSFTPLII TIMVFLGAIL ILHLNPSPLI EKAMFFVLAL VYLVSGKDVI
LGAFRGLRKG QFFDENALML IATIAAFFVG AYEESVSIMV FYSAGEFLQK LAVSRSKKSL
KALVDVAPNL AYLKKGDELV SVAPEDLRVN DIVVVKVGEK VPVDGVVVKG ESLLDERALS
GESMPVNVSE NSKVLGGSLN LKAVLEIQVE KMYKDSSIAK VVDLVQQATN EKSETEKFIT
KFSRYYTPSV LFIALMIAVL PPLFSMGSFD EWIYRGLVAL MVSCPCALVI SVPLGYFGGV
GAASRKGILM KGVHVLEVLT QAKSIAFDKT GTLTKGVFKV TDIVPQNGHS KEEVLHYASC
SQLLSTHPIA LSIQKACEEM LKDDKHQHDI KNYEEVSGMG VKAQCHTDLI IAGNEKMLDQ
FHIAHSPSKE NGTIVHVAFN QTYVGYIVIS DEIKDDAIEC LRDLKVQGIE NFCILSGDRK
SATESIAQTL GCEYHASLLP EEKTSVFKTF KERYKAPAIF VGDGINDAPT LASADVGIGM
GKGSELSKQS ADIVITNDSL NSLVKVLAIA KKTKSIIWQN ILFALGIKAV FIVLGLMGVA
SLWEAVFGDV GVTLLALANS MRAMRA
