ID   CADA_LISMN              Reviewed;         711 AA.
AC   Q60048;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 152.
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;
OS   Listeria monocytogenes.
OG   Plasmid pLm74.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=LM74;
RX   PubMed=8188605; DOI=10.1128/jb.176.10.3040-3048.1994;
RA   Lebrun M., Audurier A., Cossart P.;
RT   "Plasmid-borne cadmium resistance genes in Listeria monocytogenes are
RT   similar to cadA and cadC of Staphylococcus aureus and are induced by
RT   cadmium.";
RL   J. Bacteriol. 176:3040-3048(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LM74; TRANSPOSON=Tn5422;
RX   PubMed=8188606; DOI=10.1128/jb.176.10.3049-3061.1994;
RA   Lebrun M., Audurier A., Cossart P.;
RT   "Plasmid-borne cadmium resistance genes in Listeria monocytogenes are
RT   present on Tn5422, a novel transposon closely related to Tn917.";
RL   J. Bacteriol. 176:3049-3061(1994).
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   -!- INDUCTION: By cadmium. {ECO:0000269|PubMed:8188605}.
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; L28104; AAA25275.1; -; Genomic_DNA.
DR   RefSeq; WP_003728466.1; NZ_WUEB01000010.1.
DR   RefSeq; YP_003728018.1; NC_014255.1.
DR   PDB; 2AJ0; NMR; -; A=1-71.
DR   PDB; 2AJ1; NMR; -; A=1-71.
DR   PDBsum; 2AJ0; -.
DR   PDBsum; 2AJ1; -.
DR   AlphaFoldDB; Q60048; -.
DR   BMRB; Q60048; -.
DR   SMR; Q60048; -.
DR   TCDB; 3.A.3.6.8; the p-type atpase (p-atpase) superfamily.
DR   BRENDA; 7.2.2.21; 3045.
DR   EvolutionaryTrace; Q60048; -.
DR   PHI-base; PHI:7386; -.
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: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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cadmium; Cadmium resistance; Cell membrane;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Plasmid; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Transposable element.
FT   CHAIN           1..711
FT                   /note="Probable cadmium-transporting ATPase"
FT                   /id="PRO_0000046247"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
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        669..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          3..66
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         14
FT                   /ligand="Cd(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48775"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         17
FT                   /ligand="Cd(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48775"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   STRAND          4..11
FT                   /evidence="ECO:0007829|PDB:2AJ0"
FT   HELIX           15..27
FT                   /evidence="ECO:0007829|PDB:2AJ0"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:2AJ0"
FT   STRAND          39..48
FT                   /evidence="ECO:0007829|PDB:2AJ0"
FT   HELIX           51..58
FT                   /evidence="ECO:0007829|PDB:2AJ0"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:2AJ0"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:2AJ0"
SQ   SEQUENCE   711 AA;  77089 MW;  C23BFEB7E20CFE9A CRC64;
     MAEKTVYRVD GLSCTNCAAK FERNVKEIEG VTEAIVNFGA SKITVTGEAS IQQVEQAGAF
     EHLKIIPEKE SFTDPEHFTD HQSFIRKNWR LLLSGLFIAV GYASQIMNGE DFYLTNALFI
     FAIFIGGYSL FKEGFKNLLK FEFTMETLMT IAIIGAAFIG EWAEGSIVVI LFAVSEALER
     YSMDKARQSI RSLMDIAPKE ALVRRSGTDR MVHVDDIQIG DIMIIKPGQK IAMDGHVVKG
     YSAVNQAAIT GESIPVEKNI DDSVFAGTLN EEGLLEVAVT KRVEDTTISK IIHLVEEAQG
     ERAPAQAFVD TFAKYYTPAI IVIAALIATV PPLLFGGNWE TWVYQGLSVL VVGCPCALVV
     STPVAIVTAI GNAAKNGVLV KGGVYLEEIG GLKAIAFDKT GTLTKGVPVV TDYIELTEAT
     NIQHNKNYII MAALEQLSQH PLASAIIKYG ETREMDLTSI NVNDFTSITG KGIRGTVDGN
     TYYVGSPVLF KELLASQFTD SIHRQVSDLQ LKGKTAMLFG TNQKLISIVA VADEVRSSSQ
     HVIKRLHELG IEKTIMLTGD NQATAQAIGQ QVGVSEIEGE LMPQDKLDYI KQLKINFGKV
     AMVGDGINDA PALAAATVGI AMGGAGTDTA IETADVALMG DDLQKLPFTV KLSRKTLQII
     KQNITFSLVI KLIALLLVIP GWLTLWIAIM ADMGATLLVT LNGLRLMKVK D