CADA_ALKPO
ID CADA_ALKPO Reviewed; 723 AA.
AC P30336; D3G1Y6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 151.
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=BpOF4_21834;
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OG Plasmid pBpOF4-02.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1321115; DOI=10.1128/jb.174.15.4878-4884.1992;
RA Ivey D.M., Guffanti A.A., Shen Z., Kudyan N., Krulwich T.A.;
RT "The cadC gene product of alkaliphilic Bacillus firmus OF4 partially
RT restores Na+ resistance to an Escherichia coli strain lacking an Na+/H+
RT antiporter (NhaA).";
RL J. Bacteriol. 174:4878-4884(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4; PLASMID=pBpOF4-02;
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
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; M90750; AAA22858.1; -; Genomic_DNA.
DR EMBL; CP001880; ADC52362.1; -; Genomic_DNA.
DR PIR; D42707; D42707.
DR RefSeq; WP_012961265.1; NC_013793.1.
DR AlphaFoldDB; P30336; -.
DR SMR; P30336; -.
DR PRIDE; P30336; -.
DR EnsemblBacteria; ADC52362; ADC52362; BpOF4_21834.
DR KEGG; bpf:BpOF4_21834; -.
DR HOGENOM; CLU_001771_6_4_9; -.
DR OMA; TRGPTAM; -.
DR OrthoDB; 237367at2; -.
DR Proteomes; UP000001544; Plasmid pBpOF4-02.
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 3: Inferred from homology;
KW ATP-binding; Cadmium; Cadmium resistance; Cell membrane; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Plasmid; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..723
FT /note="Probable cadmium-transporting ATPase"
FT /id="PRO_0000046245"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..690
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 12..75
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 412
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 BINDING 26
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT CONFLICT 113
FT /note="A -> T (in Ref. 1; AAA22858)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="A -> T (in Ref. 1; AAA22858)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> T (in Ref. 1; AAA22858)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="F -> S (in Ref. 1; AAA22858)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="L -> S (in Ref. 1; AAA22858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 78204 MW; 975D709B3754D5EF CRC64;
MSDQKAITSE QEMKAYRVQG FTCANCAGKF EKNVKQLSGV EDAKVNFGAS KIAVYGNATI
EELEKAGAFE NLKVTPEKSA RQASQEVKED TKEDKVPFYK KHSTLLYASL LIAFGYLSSY
VNGEENIVTT LLFLASMFIG GLSLFKVGLQ NLLRFEFDMK TLMTVAVIGG AIIGEWAEVA
IVVILFAISE ALERFSMDRA RQSIRSLMDI APKEALVKRN GQEIMIHVDD IAVGDIMIVK
PGQKIAMDGV VVSGYSAVNQ AAITGESVPV EKTVDNEVFA GTLNEEGLLE VEITKLVEDT
TISKIIHLVE EAQGERAPSQ AFVDKFAKYY TPIIMIIAAL VAIVPPLFFD GSWETWIYQG
LAVLVVGCPC ALVISTPISI VSAIGNAAKK GVLVKGGVYL EEMGALKAIA FDKTGTLTKG
VPAVTDYNVL NKQINEKELL SIITALEYRS QHPLASAIMK KAEEENITYS DVQVEDFSSI
TGKGIKGIVN GTTYYIGSPK LFKELLTNDF DKDLEQNVTT LQNQGKTAMI IGTEKEILAV
IAVADEVRES SKEILQKLHQ LGIKKTIMLT GDNKGTANAI GGQVGVSDIE AELMPQDKLD
FIKQLRSEYG NVAMVGDGVN DAPALAASTV GIAMGGAGTD TALETADVAL MGDDLRKLPF
TVKLSRKTLN IIKANITFAI AIKFIALLLV IPGWLTLWIA ILSDMGATLL VALNGLRLMR
VKE
