ID   CADA_LISMO              Reviewed;         707 AA.
AC   P58414;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Probable cadmium-transporting ATPase {ECO:0000305};
DE            EC=7.2.2.21 {ECO:0000250|UniProtKB:P20021};
DE   AltName: Full=Cadmium-efflux ATPase {ECO:0000250|UniProtKB:P20021};
GN   Name=cadA; OrderedLocusNames=lmo1100;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- FUNCTION: Couples the hydrolysis of ATP with the export of cadmium.
CC       {ECO:0000250|UniProtKB:P20021}.
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         Evidence={ECO:0000250|UniProtKB:P20021};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20021};
CC       Multi-pass membrane protein {ECO:0000255}.
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; AL591977; CAC99178.1; -; Genomic_DNA.
DR   PIR; AD1212; AD1212.
DR   RefSeq; NP_464625.1; NC_003210.1.
DR   RefSeq; WP_010989665.1; NZ_CP023861.1.
DR   AlphaFoldDB; P58414; -.
DR   SMR; P58414; -.
DR   STRING; 169963.lmo1100; -.
DR   PaxDb; P58414; -.
DR   EnsemblBacteria; CAC99178; CAC99178; CAC99178.
DR   GeneID; 986725; -.
DR   KEGG; lmo:lmo1100; -.
DR   PATRIC; fig|169963.11.peg.1131; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_6_4_9; -.
DR   OMA; TRGPTAM; -.
DR   PhylomeDB; P58414; -.
DR   BioCyc; LMON169963:LMO1100-MON; -.
DR   Proteomes; UP000000817; 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:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Cadmium; Cadmium resistance; Cell membrane; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..707
FT                   /note="Probable cadmium-transporting ATPase"
FT                   /id="PRO_0000046246"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        666..686
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          6..69
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        398
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000305"
FT   BINDING         17
FT                   /ligand="Cd(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48775"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         20
FT                   /ligand="Cd(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48775"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ   SEQUENCE   707 AA;  76478 MW;  484E9E04BDB2D71C CRC64;
     MSKASKQTTY RVDGMSCTNC AGKFEKNVKN LEGVTDAKVN FGAGKISVYG ETSISQIEKA
     GAFENLRVTD EKDYSSKPAK KESFLKKNWH LVVSIIFIIL AFISQNISGE DSTTTIILYV
     IAIVVGGFNL FKEGFANLIK LDFTMESLMT IAIIGASIIG EWAEGSIVVI LFAFSEVLER
     YSMDKARQSI RSLMDIAPKE ALIRRDDVEQ MIAVSDIQIG DIMIIKPGQK IAMDGVVIKG
     YSAINQSAIT GESIPVEKKV DDEVFAGTLN EEGLLEVKVT KHVEDTTISK IIHLVEEAQG
     ERAPAQAFVD KFAKYYTPTI MLIALLVVVV PPLFFGGDWD TWVYQGLSLL VVGCPCSLVI
     STPVSIVSAI GNSAKNGVLV KGGIYLEEIG GLQAIAFDKT GTLTKGKPVV TDFIPYSEHM
     DEQNSLSIIT ALETMSQHPL ASAIISKAMI DNVDYKSIEI DNFSSITGKG VKGEVNGITY
     YIGSSKLFES SLEKSQSISQ TYQSLQKQGK TAMLFGTESN ILAIIAVADE VRESSKEVIA
     QLHKLGIAHT IMLTGDNNDT AQFIGKEIGV SDIKAELMPE DKLTYIKELK QTYGKVAMIG
     DGVNDAPALA ASTVGIAMGG AGTDTALETA DVALMGDDLK KLPFIVNLSR KTLKIIKQNI
     TFSLGIKLLA LLLVLPGWLT LWIAIVADMG ATLLVTLNGL RLMKVKK