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Database: UniProt
Entry: A0A1I5BTT3_9FIRM
LinkDB: A0A1I5BTT3_9FIRM
Original site: A0A1I5BTT3_9FIRM 
ID   A0A1I5BTT3_9FIRM        Unreviewed;       637 AA.
AC   A0A1I5BTT3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE            EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN   ORFNames=SAMN04489757_101212 {ECO:0000313|EMBL:SFN78077.1};
OS   Anaerocolumna aminovalerica.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerocolumna.
OX   NCBI_TaxID=1527 {ECO:0000313|EMBL:SFN78077.1, ECO:0000313|Proteomes:UP000198806};
RN   [1] {ECO:0000313|EMBL:SFN78077.1, ECO:0000313|Proteomes:UP000198806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1283 {ECO:0000313|EMBL:SFN78077.1,
RC   ECO:0000313|Proteomes:UP000198806};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FOWD01000001; SFN78077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5BTT3; -.
DR   STRING; 1527.SAMN04489757_101212; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000198806; 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; cd07548; P-type_ATPase-Cd_Zn_Co_like; 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 HMA2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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   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   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:UP000198806};
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        9..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        39..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        247..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        281..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        585..604
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        610..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   637 AA;  68536 MW;  302B8F7A65316427 CRC64;
     MTKKEKRLLI RILIAGAIFF LAVPIHYREH IYKALGWGFL QSPIISYIEF PAFLIAYLII
     GGEIVRKALK NISKGQIFDE NFLMSVATIG AFCLGEYAEG VAVMLFYQVG ELFQSYAVSR
     SRRSIAELMD IRPDYANVLR NGELVQVDPE EVAIGDTIVV KPGERIPLDG VVTDGRSALD
     TSALTGESVP RDVNTGDEVI SGCINQTGKL IIKVSKEFGE STVSKILELV ENASDKKSKS
     ENFITRFARY YTPFVVFAAV ALSIIPPLVT GQSFLIWIER ALTFLVISCP CALVISVPLS
     FFGGIGGASK CGVLVKGSNY LELLADTETV VFDKTGTLTK GNFVVSEVRA LNMSKEELIE
     IAAHAEDYSS HPIAASIRKA YGKTVDSSLI KDIEEIAGHG VKAVINDRVV LAGNAKLMKL
     KGISYEETSS VGTVVHIAID GAYAGYIVIA DEIKADSRQA ILDLKAAGVK QTVMLTGDAD
     AVGKKVAAQL NLDKTYTELL PADKVDQLEK LMKQKSEKAM LAFVGDGIND APVLARADVG
     IAMGGLGSDA AIEAADVVIM TDEPSKIATV MKISRKTLRI VKQNIVFALF VKGVVLVLGA
     VGLANMWGAV FADVGVSIIA ILNAIRALNV TKYSQSH
//
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