HMCT_HELFE
ID HMCT_HELFE Reviewed; 681 AA.
AC Q9RQB4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cadmium, zinc and cobalt-transporting ATPase;
DE EC=7.2.2.12;
DE EC=7.2.2.21;
GN Name=cadA;
OS Helicobacter felis.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=214;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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. {ECO:0000250}.
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; AF125316; AAF12735.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RQB4; -.
DR SMR; Q9RQB4; -.
DR GeneID; 36133968; -.
DR OMA; IVTWLFM; -.
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 GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
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; 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; 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 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; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cadmium; Cell membrane; Cobalt; Cobalt transport; Copper;
KW Copper transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..681
FT /note="Cadmium, zinc and cobalt-transporting ATPase"
FT /id="PRO_0000046175"
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..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 631..652
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 653..660
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 661..676
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 677..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 1..66
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 578
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 582
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 681 AA; 73748 MW; 913834388D4FBC5B CRC64;
MQKYHFTGLD CPDCANKLES ALNKQSYVQE ARVVFNTNTL YLKTQDMPKA LALIKQLEPD
MELSEQVQSE AKPSAIPLLL SVVLYLIAVA TIHFSAQNWA LHLSYALLAG VYLVAGKDVF
LGALRAIRNK QFFDENTLML SATIAAFGVG AHEEAVSIMV FYSAGEFLQQ LAIARSKQSL
HALLDVAPNH AVRKVGQELQ EVEPSALAIG DVVIVKVGEK IPTDGVVLRG ESLLDQKALT
GESLPVNVKE HSAVLGGSIN LKGVLEIQVS KLYADSSVAK IVDLVSNAVS QKSQTEKFIT
TFARYYTPAV FAIALLIALV PPLLGHGDFD TWIYRGLFAL MVSCPCALVI SVPLGYFGGV
GAASRAGILI KSVQTLEALS QVKNIAFDKT GTLSKGEFNV IDVVPIAPFS KEDVLQHATC
AQILSTHPIA ISIQKAYKRQ CQHEVKDYQE IGGLGVQASC HSHLIIAGND KMLHKYNIPH
DTCSLEGTIV HVAVDGKHIG YIVVADTLKD NAKECLDGLK HAGIEHMCIL SGDHEYSTKR
VAKELDCPYY ANLLPEDKLN AFKDFQAQHA HKSMFVGDGI NDAPTLARAD VSMSMGSASQ
ISKESADIVI TNNSLESVLK VFKIAKKTKR IIIENIIFAL AIKAMFIVLG LSGDASLWEA
VLGDVGVTLI ALANSMRTMR I
