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Database: UniProt
Entry: A0A1M4M3E9_9FIRM
LinkDB: A0A1M4M3E9_9FIRM
Original site: A0A1M4M3E9_9FIRM 
ID   A0A1M4M3E9_9FIRM        Unreviewed;       617 AA.
AC   A0A1M4M3E9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE            EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN   Name=zntA3 {ECO:0000313|EMBL:SCG82181.1};
GN   ORFNames=DW1_0570 {ECO:0000313|EMBL:SCG82181.1};
OS   Proteiniborus sp. DW1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX   NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG82181.1, ECO:0000313|Proteomes:UP000185208};
RN   [1] {ECO:0000313|EMBL:SCG82181.1, ECO:0000313|Proteomes:UP000185208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW1 {ECO:0000313|EMBL:SCG82181.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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; FMDO01000008; SCG82181.1; -; Genomic_DNA.
DR   RefSeq; WP_074349129.1; NZ_FMDO01000008.1.
DR   AlphaFoldDB; A0A1M4M3E9; -.
DR   STRING; 1889883.DW1_0570; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000185208; 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; cd02079; 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; TIGR01511; ATPase-IB1_Cu; 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; 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:SCG82181.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000185208};
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        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        35..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        63..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        86..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        234..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        258..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        567..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        593..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   617 AA;  66620 MW;  E3A66EB216F1C556 CRC64;
     MQRQILSNKN KIVLFSGILI AVGFLSKWTM DNIYIFEWSL IIASILGLAP IAIQAIQALR
     VKVVSIDVLV TIAVVSAFLI QNYEESAIVT FLFLFGAFLE QRTLNKTRSA IKELTEMAPE
     SALKQMGNGE FEEVEVDEVD VGDVLLVKTG AKVPVDGTVL SGEASINEAS ITGESLPVRK
     EKGSNVFAGT ILDNGTIQVV ADRVGEDTTF GKIIELVEEA QDSKSEAERF IDRFSKYYTP
     VVLVLSFIVW LFSRDIELAI TILVLGCPGA LVIGVPVSNV AGIGNGARHG ILLKGSEVIR
     DFSRLDTMVF DKTGTLTVGN PSVAEKEYYG DEIDEVLGYL ASVERESDHP LAKAVLEEIG
     ETTFSPVENT EVIKGGGIVA KVNGHRIAVG NITLMERENV ELDEKAKADV ESLEKNGNSL
     VLTAVDGKLK VLMGVRDQIR SGVKEDLLKL KKLGVKKLVM LSGDNQGTVD LVSRELGLTE
     AHGNMLPGDK SVYIKKLIEE GQIVAFVGDG VNDSPSLALA NIGIAMGGGT DVAIETSDVV
     LMNSDFSCLP HALGLTKAIA RNMKQNIFIA VGVVLVLLAS VLFSEWMNMS IGMLVHEGSI
     LAVILNGMRL LRYNLRK
//
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