ID A0A285D3S4_9BACI Unreviewed; 720 AA.
AC A0A285D3S4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN ORFNames=SAMN05877753_109137 {ECO:0000313|EMBL:SNX74477.1};
OS Bacillus oleivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1448271 {ECO:0000313|EMBL:SNX74477.1, ECO:0000313|Proteomes:UP000219546};
RN [1] {ECO:0000313|EMBL:SNX74477.1, ECO:0000313|Proteomes:UP000219546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC228 {ECO:0000313|EMBL:SNX74477.1,
RC ECO:0000313|Proteomes:UP000219546};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00036510};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; OAOP01000009; SNX74477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285D3S4; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000219546; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd07545; P-type_ATPase_Cd-like; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 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 {ECO:0000256|RuleBase:RU362081};
KW Cadmium {ECO:0000256|ARBA:ARBA00022539};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000219546};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 101..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 124..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 358..382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 10..73
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 720 AA; 77737 MW; 66857FE5E9923918 CRC64;
MNEVTEALER KTVYRVEGFS CANCAGKFER NVKQLPGVQD ARVNFGASKI SVYGSTTIED
LEKAGAFENL KVTPENPVQV QGTNQAAEKE AKEPIYKKHS TLLFASLLIV FGYVSQFVNG
EDNLVTSLLF AAAIVIGGFS LFKVGFQNLS HLEFDMKTLM TVAVIGAAII GEWAEGAIVV
ILFAISEALE RFSMDRARQS IRSLMDIAPK EALVRRNGQE LMVHVDQIAV GDIMIVKPGQ
KIAMDGIVVK GYSAVNQAAI TGESVPVEKT AGNEVFAGTL NEEGLLEVKV TKLVDDTTIA
KIIHLVEEAQ GERAPSQAFV DKFAKYYTPA IMAIAALVAV IPPLLINGSW QTWVYQGLAV
LVVGCPCALV ISTPISIVSA IGNAAKNGVL IKGGIYLEQM GIIKAMAFDK TGTLTKGVPV
VTDFKIINNK MSENQLFTLI AALEKRSGHP LASAIVKKAE EANISFADVM VEDFTSITGK
GIQGTINSTT YYIGSPQLFE EFQTTVFDKS LQQQIQELQQ QGKTVMAAGT KEEILAFLAV
ADEVREESKE VMEKLHQMGI EQTVMLSGDN KSTSNAIGKN VGVTEIQAEL LPEDKLTFIQ
NLRSEYKHVA MVGDGVNDAP ALAASTVGIA MGGAGTDTAL ETADVALMGD DLKKLPFTIK
LSRKALNIIK QNIMFSISIK VLALLLVVPN WLTLWIAVLA DMGATILVTL NSLRLLRVRE
//
