ID A0A3D8YTV3_9BACL Unreviewed; 873 AA.
AC A0A3D8YTV3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN Name=cadA {ECO:0000313|EMBL:REB04767.1};
GN ORFNames=DVB69_16930 {ECO:0000313|EMBL:REB04767.1};
OS Sporosarcina sp. BI001-red.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=2282866 {ECO:0000313|EMBL:REB04767.1, ECO:0000313|Proteomes:UP000256461};
RN [1] {ECO:0000313|EMBL:REB04767.1, ECO:0000313|Proteomes:UP000256461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI001-red {ECO:0000313|EMBL:REB04767.1,
RC ECO:0000313|Proteomes:UP000256461};
RA Rajandas H., Sivachandran P., Mai C.W., Cheong K.W., Teh C.S.J.,
RA Lim E.S.H., Yap I.K.S., Convey P., Chong C.W.;
RT "Draft Genome of Sporosarcina subantarcticus.";
RL Submitted (JUL-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:REB04767.1}.
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DR EMBL; QQAK01000017; REB04767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8YTV3; -.
DR OrthoDB; 9766480at2; -.
DR Proteomes; UP000256461; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:RHEA.
DR CDD; cd00371; HMA; 2.
DR Gene3D; 3.30.70.100; -; 2.
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; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
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 Hydrolase {ECO:0000313|EMBL:REB04767.1};
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:UP000256461};
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 260..277
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 485..504
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 516..541
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 825..841
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 106..171
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 178..241
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 873 AA; 94316 MW; 09C8574094E17B99 CRC64;
MDKKCCSTNT EPQKVEEQTN CCSSTQDTQI EKKQGVTTNC CSSNTIDTGA EDECCNKDSM
IIKEDSKGTT CCNSKELEKA TIGADDCCAQ PKELLNPVNG NLDEGVKEEF RVNGMDCPAC
AVTIEKSLRT QPNIIGVHVN YSTGKMQVSS TKELEFESIQ KQMKKLGFEV EPIKVNNNLK
NYFIEGMDCG SCALTIENHL NHLPTVKYVQ VNFATGKMKI EHVNSPEEII NEVAKAGFIA
SLITNNNQTP SPTRSINQNG AVIFSGILIA LGFIGSHTGV SPYLTITMYA VALVISGYKP
VKSAYYAIRS RSLDMNVLMS AAAIGAAFLG EWLEGATVVW LFALGLNLQN RAIEKTRKSI
RGLMELTPPE AWVQVGNELI RKPVEEISIH DVIVVKPGDR IPLDGDVIEG ESSVNQAAIT
GESIPVDKEK GSFVYAGSLN EHGSLSVRVT KLIEDTTIAK IIHLVEEAQE QKAPTEAFID
KFARIYTPVV FILALLVMLV PPLFGFGTWD EWIYKGLTLL VIACPCALVI STPVAIVSAL
GNAAKNGVLI KGGTFLENAG TINAIAFDKT GTLTEGKPKV TDVVVFNDSE ETLLSIARTL
EEYSTHPIAK TIVDYAKGKG IQAKSGSEFK NLAGKGIQAT IDHVPYFAGN KKLFKEVNTP
IDNHLEEISR LQDEGKTIII IGTAEKILGI MCVSDTIRKA TKVAIANLEK IGVEQVVMLT
GDNEGTAKAI ALEAGVNRYF SELLPEEKVD AIKKLQEEGY RVAMVGDGIN DAPALATANL
GIAMGGAGTD TAMETADIVL MADNLEKLPH TIKLSRKALS IIKQNIWFSI LIKVVALLLI
LPGLLTLWVA VLSDTGAALI VILNALRLLK VKG
//
