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Database: UniProt
Entry: J0AL92_HELPX
LinkDB: J0AL92_HELPX
Original site: J0AL92_HELPX 
ID   J0AL92_HELPX            Unreviewed;       686 AA.
AC   J0AL92;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Cadmium-translocating P-type ATPase {ECO:0000313|EMBL:EJC56917.1};
DE            EC=3.6.3.3 {ECO:0000313|EMBL:EJC56917.1};
GN   Name=cadA {ECO:0000313|EMBL:EJC56917.1};
GN   ORFNames=HPHPP3B_0898 {ECO:0000313|EMBL:EJC56917.1};
OS   Helicobacter pylori Hp P-3b.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=992100 {ECO:0000313|EMBL:EJC56917.1, ECO:0000313|Proteomes:UP000004225};
RN   [1] {ECO:0000313|EMBL:EJC56917.1, ECO:0000313|Proteomes:UP000004225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hp P-3b {ECO:0000313|EMBL:EJC56917.1,
RC   ECO:0000313|Proteomes:UP000004225};
RA   Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA   Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT   "Genome sequence of Helicobacter pylori Hp P-3b.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC       ECO:0000256|RuleBase:RU362081}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJC56917.1}.
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DR   EMBL; AKQC01000004; EJC56917.1; -; Genomic_DNA.
DR   RefSeq; WP_001158805.1; NZ_AKQC01000004.1.
DR   AlphaFoldDB; J0AL92; -.
DR   PATRIC; fig|992100.3.peg.875; -.
DR   Proteomes; UP000004225; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 1.
DR   CDD; cd07548; P-type_ATPase-Cd_Zn_Co_like; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM/ZINC-TRANSPORTING ATPASE HMA4-RELATED; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Hydrolase {ECO:0000313|EMBL:EJC56917.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        73..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        136..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        332..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        641..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..62
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   686 AA;  74798 MW;  18974F74D48F5CA3 CRC64;
     MQEYHIHNLD CPDCAAKLER DLNKLDYVKK AQINFSTSKL FLDTSDFEKV RAFIKQNEPH
     LSLSFKEAAE KPLSFTPLIV TIAVFLGAIL ILHLEPSPFI EKAVFVVLAL VYLISGKDVI
     LGAFRGLRKG QFFDENALML IATIAAFCVG AYEESVSIMV FYSAGEFLQK LAIARSKKSL
     KALVDVAPNL AYLKKGDTLV SVAPEDLRIN DIVVVKVGEK VPVDGVVIKG ESLLDERALS
     GESMPVNVSE NSKVLGGSLN LKAVLEIQVE KLYKDSSIAK VVDLVQQATN EKSETEKFIT
     KFSRYYTPSV LFIALMIAVL PPLFSMGSFD EWIYRGLVAL MVSCPCALVI SVPLGYFGGV
     GAASRKGILM KGVHVLEVLT QAKSIAFDKT GTLTKGVFKV TDIVPQNGHS KEEVLHYASC
     SQLLSTHPIA LSIQKACEEM LKDDKHQHDI KNYEEVSGMG VKAQCHTDLI IAGNEKMLDQ
     FHIAHSPSKE NGTIVHVAFN QTYIGHIVIS DEIKDDAIEC LRDLKAQGIE NFCILSGDRK
     SATESIAQTL GCEYHASLLP EEKTSVFKTF KERYKAPAIF VGDGINDAPT LASADVGIGM
     GKGSELSKQS ADIVITNDSL NSLVKVLAIA KKTKSIIWQN ILFALGIKAV FIVLGLMGVA
     SLWEAVFGDV GVTLLALANS MRAMRA
//
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