CADA1_STAAU
ID CADA1_STAAU Reviewed; 727 AA.
AC P20021;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cadmium-transporting ATPase {ECO:0000303|PubMed:1530844};
DE EC=7.2.2.21 {ECO:0000269|PubMed:1530844};
DE AltName: Full=Cadmium-efflux ATPase {ECO:0000303|PubMed:2524829};
GN Name=cadA {ECO:0000303|PubMed:2524829};
OS Staphylococcus aureus.
OG Plasmid pI258.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=BD224;
RX PubMed=2524829; DOI=10.1073/pnas.86.10.3544;
RA Nucifora G., Chu L., Misra T.K., Silver S.;
RT "Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene
RT results from a cadmium-efflux ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3544-3548(1989).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RX PubMed=1530844; DOI=10.1128/jb.174.1.116-121.1992;
RA Tsai K.J., Yoon K.P., Lynn A.R.;
RT "ATP-dependent cadmium transport by the cadA cadmium resistance determinant
RT in everted membrane vesicles of Bacillus subtilis.";
RL J. Bacteriol. 174:116-121(1992).
CC -!- FUNCTION: Couples the hydrolysis of ATP with the export of cadmium
CC (PubMed:1530844). Involved in cadmium resistance (PubMed:2524829,
CC PubMed:1530844). {ECO:0000269|PubMed:1530844,
CC ECO:0000269|PubMed:2524829}.
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:0000269|PubMed:1530844};
CC -!- ACTIVITY REGULATION: Inhibited by the antibiotic bafilomycin A1.
CC Partially inhibited by DCCD, nigericin and FCCP.
CC {ECO:0000269|PubMed:1530844}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1530844};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: By cadmium. {ECO:0000269|PubMed:1530844}.
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; J04551; AAB59154.1; -; Genomic_DNA.
DR PIR; A32561; A32561.
DR RefSeq; WP_000003267.1; NZ_UHCF01000003.1.
DR RefSeq; YP_006937600.1; NC_013319.1.
DR RefSeq; YP_006938635.1; NC_013347.1.
DR RefSeq; YP_006938768.1; NC_013352.1.
DR AlphaFoldDB; P20021; -.
DR SMR; P20021; -.
DR TCDB; 3.A.3.6.1; the p-type atpase (p-atpase) superfamily.
DR PRIDE; P20021; -.
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 ATP-binding; Cadmium; Cadmium resistance; Cell membrane; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Plasmid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..727
FT /note="Cadmium-transporting ATPase"
FT /id="PRO_0000046248"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 12..75
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 415
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 23
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000305"
FT BINDING 26
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280,
FT ECO:0000305"
SQ SEQUENCE 727 AA; 78812 MW; 7281664ED658FBE9 CRC64;
MSEQKVKLME EEMNVYRVQG FTCANCAGKF EKNVKKIPGV QDAKVNFGAS KIDVYGNASV
EELEKAGAFE NLKVSPEKLA NQTIQRVKDD TKAHKEEKTP FYKKHSTLLF ATLLIAFGYL
SHFVNGEDNL VTSMLFVGSI VIGGYSLFKV GFQNLIRFDF DMKTLMTVAV IGATIIGKWA
EASIVVILFA ISEALERFSM DRSRQSIRSL MDIAPKEALV RRNGQEIIIH VDDIAVGDIM
IVKPGEKIAM DGIIVNGLSA VNQAAITGES VPVSKAVDDE VFAGTLNEEG LIEVKITKYV
EDTTITKIIH LVEEAQGERA PAQAFVDKFA KYYTPIIMVI AALVAVVPPL FFGGSWDTWV
YQGLAVLVVG CPCALVISTP ISIVSAIGNA AKKGVLVKGG VYLEKLGAIK TVAFDKTGTL
TKGVPVVTDF EVLNDQVEEK ELFSIITALE YRSQHPLASA IMKKAEQDNI PYSNVQVEEF
TSITGRGIKG IVNGTTYYIG SPKLFKELNV SDFSLGFENN VKILQNQGKT AMIIGTEKTI
LGVIAVADEV RETSKNVIQK LHQLGIKQTI MLTGDNQGTA NAIGTHVGVS DIQSELMPQD
KLDYIKKMQS EYDNVAMIGD GVNDAPALAA STVGIAMGGA GTDTAIETAD IALMGDDLSK
LPFAVRLSRK TLNIIKANIT FAIGIKIIAL LLVIPGWLTL WIAILSDMGA TILVALNSLR
LMRVKDK
