ID   P94888_9LACT            Unreviewed;       705 AA.
AC   P94888;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   04-NOV-2026, entry version 148.
DE   RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE            EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN   Name=cadA {ECO:0000313|EMBL:AAB37345.1};
OS   Lactococcus lactis.
OG   Plasmid pND302 {ECO:0000313|EMBL:AAB37345.1}.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1358 {ECO:0000313|EMBL:AAB37345.1};
RN   [1] {ECO:0000313|EMBL:AAB37345.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M71 {ECO:0000313|EMBL:AAB37345.1};
RC   PLASMID=pND302 {ECO:0000313|EMBL:AAB37345.1};
RA   Liu C.-Q., Chia G.L., Dunn N.W.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAB37345.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M71 {ECO:0000313|EMBL:AAB37345.1};
RC   PLASMID=pND302 {ECO:0000313|EMBL:AAB37345.1};
RX   PubMed=9339465; DOI=10.1006/plas.1997.1301;
RA   Liu C.Q., Khunajakr N., Chia L.G., Deng Y.M., Charoenchai P., Dunn N.W.;
RT   "Genetic analysis of regions involved in replication and cadmium resistance
RT   of the plasmid pND302 from Lactococcus lactis.";
RL   Plasmid 38:79-90(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cd(2+)(in) + ATP + H2O = Cd(2+)(out) + ADP + phosphate + H(+);
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         Evidence={ECO:0000256|ARBA:ARBA00049338};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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}.
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DR   EMBL; U78967; AAB37345.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94888; -.
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:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008551; F:P-type cadmium transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd00371; HMA; 1.
DR   CDD; cd07545; P-type_ATPase_Cd-like; 1.
DR   FunFam; 2.70.150.10:FF:000002; Copper-transporting ATPase 1, putative; 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; IPR059000; ATPase_P-type_domA.
DR   InterPro; IPR051014; Cation_Transport_ATPase_IB.
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; TIGR01511; ATPase-IB1_Cu; 1.
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; SFLDS00003; Haloacid_Dehalogenase; 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; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362081};
KW   Cadmium {ECO:0000256|ARBA:ARBA00022539};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU362081};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
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|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362081};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:AAB37345.1};
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}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   TRANSMEM        89..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        113..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        143..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        166..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        654..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        680..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          6..69
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   705 AA;  76467 MW;  DFF07A0DC41AF325 CRC64;
     MSEKMTEKTY RIEGLSCTNC AGKFEKNVKQ LPGVTSATVN FGASKISVEG QTTIEELEEA
     GAFENLIIRD DQENDEQVRS KESFIKRNIA LIISLGFILV AVISQLSLGE DHLLTKALYI
     LAIIIGGFDL FKEGFSDLIK LDFSMESLMT IAIIGAAFIG EWAEGSIVVI LFAISEALER
     FSMDKARQSI RSLMDIAPKE ALIRRNNVEQ LVSVDKIDID DIMIIKPGQK IAMDGLVING
     HSSVNQAAIT GESVPVEKQL DDEVFAGTLN EEGILEVKVT KKVTDTTIAK IIHLVEEAQG
     ERAPAQAFVD KFAKYYTPFI IIMALLIVVV PPLFFGGDWN KWLYQGLSIL VVGCPCSLVI
     STPVSIVSAI GNAAKNGVLV KGGVYLEEIG HLRAIAFDKT GTLTKGKPVV TDFIATSSET
     DINYLSIISS LESLSQHPLA SAILNEADKT NVDYKSIQIE DFQSITGKGL TGIHQNIRYY
     IGSPKLFSAS VIEETAVKVQ YRQFQEQGKT AMYFGTDEQI LGVIAVADEV RDSSAAVISE
     LHKLSIEHTI MLTGDNTKTA ESIGKQLGVT EIKGDLMPQE KLDSIKALRT TYNKVAMVGD
     GINDAPALAA STVGIAMGGA GTDTALETAD VALMGDDLQK LPFIVRLSRQ TLKVIKQNIT
     FSLGIKLLAL LLVIPGWLTL WIAIVADMGA TLLVTLNGLR LMKVK
//