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
//