ID A0A3R5V1F3_LATCU Unreviewed; 597 AA. AC A0A3R5V1F3; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 24-JAN-2024, entry version 17. 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:QAR35601.1}; GN ORFNames=EQK21_05850 {ECO:0000313|EMBL:QAR35601.1}; OS Latilactobacillus curvatus (Lactobacillus curvatus). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Latilactobacillus. OX NCBI_TaxID=28038 {ECO:0000313|EMBL:QAR35601.1, ECO:0000313|Proteomes:UP000286835}; RN [1] {ECO:0000313|EMBL:QAR35601.1, ECO:0000313|Proteomes:UP000286835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SRCM103465 {ECO:0000313|EMBL:QAR35601.1, RC ECO:0000313|Proteomes:UP000286835}; RA Kong H.-J., Jeong S.-Y., Jeong D.-Y.; RT "Genome sequence of Lactobacillus curvatus SRCM103465."; RL Submitted (JAN-2019) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP035110; QAR35601.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3R5V1F3; -. DR Proteomes; UP000286835; Chromosome. 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; cd07544; P-type_ATPase_HM; 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; IPR027256; P-typ_ATPase_IB. DR InterPro; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. 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 HMA4-RELATED; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00120; HATPASE. 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 PROSITE; PS00154; ATPASE_E1_E2; 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 Hydrolase {ECO:0000313|EMBL:QAR35601.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081}; KW Metal-binding {ECO:0000256|RuleBase:RU362081}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081}; 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}. FT TRANSMEM 6..25 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT TRANSMEM 32..50 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT TRANSMEM 227..246 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT TRANSMEM 252..273 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" FT TRANSMEM 551..578 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362081" SQ SEQUENCE 597 AA; 63283 MW; 20CB4EE6729BB2C9 CRC64; MKHTIKFALT ISVGVIALCL AFLLHEPLWA QILVSLAGSL VALSMFIEMI KTLKSGQYGV DLLAITAIIA TLAVGEYWAA LMVLVMLTGG DSLEDYAAHK AGRELKTLLD NSPQTAHRLV NDAVEDVSVD KLQVGDQVII KPGELVPVDG HIIAGSALFD ESSLTGESRP VEKALNDELM SGSVNGDTSV TMQVDQLAIN SQYQAIVRLV ETSAAQPAHF VRLADRYAVP FTLVAYVIAG VAWWLSKDPV RFAEVLVVAS PCPLILAAPI ALISGMSRAS RNGIIVKAGT TIEKLASAKS AAFDKTGTIT NGQLTVDQVV PVIGIAPTEL LQLAASAEQE SSHILARSLV KAAQVEQLQP IETLKEATGA GVVATLSSGQ MVRVGKHQFV TPDAQQPLQE QTTVYVAINE QYAGYITFID HLRPEAPATM QTLHQLGITR LMMLTGDQAT TAHQIAEQVG IDDVHAGCLP VDKIHLIEQV PQDQRPLIMV GDGVNDAPSL ASADVGIAMG AHGATAASES ADVVILKDDL GRVSRAVQIA RDTMRVARQA VLIGIAICIG LMLIASTGIV PALVGALFQE VVDTVSILYA LRARTDR //