CADA_STAAR
ID CADA_STAAR Reviewed; 726 AA.
AC Q6GIX1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=SAR0723;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
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DR EMBL; BX571856; CAG39734.1; -; Genomic_DNA.
DR RefSeq; WP_000378396.1; NC_002952.2.
DR AlphaFoldDB; Q6GIX1; -.
DR SMR; Q6GIX1; -.
DR KEGG; sar:SAR0723; -.
DR HOGENOM; CLU_001771_6_4_9; -.
DR OMA; TRGPTAM; -.
DR OrthoDB; 237367at2; -.
DR Proteomes; UP000000596; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0055072; P:iron ion homeostasis; 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; Cell membrane; Ion transport; Iron; Iron transport;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..726
FT /note="Probable cadmium-transporting ATPase"
FT /id="PRO_0000225595"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 11..74
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 414
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 25
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ SEQUENCE 726 AA; 78361 MW; E78D9DF405057438 CRC64;
MDSSAKTLTE DKQVYRVEGF SCANCAGKFE KNVKQLAGVQ DAKVNFGASK IDVYGNASVQ
ELEKAGAFEN LKVFPEKLAN SSMQAVKEDT KAPKEEKIPF YKKHSTLLFA TLLIAFGYLS
HFVNGEDNLV TSMLFVGSIV IGGYSLFKVG FQNLIRFDFD MKTLMTVAVI GAAIIGEWAE
ASIVVVLFAI SEALERFSMD RARQSIRSLM DIAPKEALVM RNGQEIMIHV DDIAVGDIMI
VKPGEKIAMD GIIINGVSAV NQAAITGESV PVAKTVDDEV FAGTLNEEGL LEVKITKYVE
DTTISKIIHL VEEAQGERAP AQAFVDKFAK YYTPIIMVIA ALVAVVPPLF FGGSWDTWVY
QGLAVLVVGC PCALVISTPI SIVSAIGNAA KKGVLIKGGV YLEELGAIKA IAFDKTGTLT
KGVPVVTDFK VLNDQVEEKE LFSIITALEY RSQHPLASAI MKKAEQDNIT YSDVRVEDFT
SITGRGIQGN IDGTTYYIGS PRLFKELNVS DFSLEFENKV KVLQNQGKTA MIIGTDQTIL
GVIAVADEVR ETSKNVIQKL HQLGIKQTIM LTGDNQGTAE AIGAHVGVSD IQSELMPQDK
LDYIKKMKAE HGNVAMIGDG VNDAPALAAS TVGIAMGGAG TDTAIETADI ALMGDDLSKL
PFAVRLSRKT LNIIKANITF AIGIKIIALL LVIPGWLTLW IAILSDMGAT ILVALNSLRL
MRVKDK
