CADA2_STAAU
ID CADA2_STAAU Reviewed; 804 AA.
AC P37386; Q7DIB0; Q93ID4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 131.
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 Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=PsiTn554;
RA Chikramane S.G., Dubin D.T.;
RT "PsiTn554: a Staphylococcus aureus chromosomal element encoding cadmium
RT resistance determinants, and genes resembling the transposases genes of
RT Tn554.";
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=85/2082, and 85/3907;
RX PubMed=11302791; DOI=10.1128/aac.45.5.1323-1336.2001;
RA Ito T., Katayama Y., Asada K., Mori N., Tsutsumimoto K.;
RT "Structural comparison of three types of staphylococcal cassette chromosome
RT mec integrated in the chromosome in methicillin-resistant Staphylococcus
RT aureus.";
RL Antimicrob. Agents Chemother. 45:1323-1336(2001).
CC -!- FUNCTION: Couples the hydrolysis of ATP with the export of cadmium.
CC Involved in cadmium resistance. {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}.
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DR EMBL; L10909; AAA26610.1; -; Genomic_DNA.
DR EMBL; AB047089; BAC57487.1; -; Genomic_DNA.
DR EMBL; AB037671; BAB47609.1; -; Genomic_DNA.
DR RefSeq; WP_000378485.1; NZ_WBTV01000056.1.
DR RefSeq; WP_000378487.1; NZ_UGZU01000004.1.
DR AlphaFoldDB; P37386; -.
DR SMR; P37386; -.
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; 2.
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; 2.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 2.
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; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cadmium; Cadmium resistance; Cell membrane; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Repeat; Translocase; Transmembrane; Transmembrane helix; Transport;
KW Transposable element.
FT CHAIN 1..804
FT /note="Probable cadmium-transporting ATPase"
FT /id="PRO_0000046249"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..771
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 776..798
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 11..74
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 89..152
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 492
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 22
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 25
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 100
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 103
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT VARIANT 135
FT /note="A -> T (in strain: 85/2082)"
SQ SEQUENCE 804 AA; 86883 MW; D8D26DE6EB878026 CRC64;
MDSSTKTLTE DKQVYRVEGF SCANCAGKFE KNVKELSGVH DAKVNFGASK IDVFGSATVE
DLEKAGAFEN LKVAPEKARR RVEPVVTEDK NVYRVEGFSC ANCAGKFEKN VKQLAGVQDA
KVNFGASKID VYGNASVEEL EKAGAFENLK VIPEKLANPS IQAVKEDTKA PKEEKIPFYK
KHSTLLFATL LIAFGYLSHF VNGEDNLVTS MLFVSSIVIG GYSLFKVGFQ NLIRFDFDMK
TLMTVAVIGA AIIGEWAEAS IVVILFAISE ALERFSMDRA RQSIRSLMDI APKEALVRRN
GQEIMIHVDD IAVGDIMIVK PGEKIAMDGI IINGVSAVNQ AAITGESVPV AKTVDDEVFA
GTLNEEGLLE VKITKYVEDT TISKIIHLVE EAQGERAPAQ AFVDKFAKYY TPIIMVIAAL
VAVVPPLFFG GSWDTWVYQG LAVLVVGCPC ALVITTPISI VSAIGNAAKK GVLIKGGVYL
EELGAIKAIA FDKTGTLTKG VPVVTDFKVL NDQVEEKELF SIITALEYRS QHPLASAIMK
KAEQDNITYS DVRVKDFTSI TGRGIQGNID GTTYYIGSPR LFKELNVSDF SLEFENKVKV
LQNQGKTAMI IGTDQTILGV IAVADEVRET SKNVILKLHQ LGIKQTIMLT GDNQGTAEAI
GAHVGVSDIQ SELLPQDKLD YIKKMKAEHG NVAMIGDGVN DAPALAASTV GIAMGGAGTD
TAIETADIAL MGDDLSKLPF AVRLSRKTLN IIKANITFAI GIKIIALLLV IPGWLTLWIA
ILSDMGATIL VALNSLRLMR VKDK
