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Database: UniProt
Entry: A0A1I1YR29_9FIRM
LinkDB: A0A1I1YR29_9FIRM
Original site: A0A1I1YR29_9FIRM 
ID   A0A1I1YR29_9FIRM        Unreviewed;       739 AA.
AC   A0A1I1YR29;
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=SAMN02910278_00295 {ECO:0000313|EMBL:SFE21899.1};
OS   Peptostreptococcus sp. D1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptostreptococcus.
OX   NCBI_TaxID=72304 {ECO:0000313|EMBL:SFE21899.1, ECO:0000313|Proteomes:UP000199190};
RN   [1] {ECO:0000313|EMBL:SFE21899.1, ECO:0000313|Proteomes:UP000199190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1 {ECO:0000313|EMBL:SFE21899.1,
RC   ECO:0000313|Proteomes:UP000199190};
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; FONP01000001; SFE21899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1YR29; -.
DR   STRING; 72304.SAMN02910278_00295; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000199190; 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   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; 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; 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   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; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 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   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:UP000199190};
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        119..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        349..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        376..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        688..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        713..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..70
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   739 AA;  80540 MW;  089606E6E95BA114 CRC64;
     MKVEIILGGL NCAHCAGVIE EKVKKMESVD SASLNFVSKK LIANIKDNEN VAEQIGYIRN
     IIDTTEPGLK IEVLGQGTEN NFDRESKSES CSCSSSCSLC SSESDKSNRS IFRIENEENL
     KIISIAVAVI FSLSAYVFNS VLENYIVANA LFVVAYFVAG YEVLGDAIRN ILKGKLMDEN
     FLMSVATIGA LIIGEYPEAV GVMVFYSIGE LLESHAVSKS RKDIESLMDI KPDVANLLID
     GEIVRVSPES VNIGDIIVVR VGEKVPLDGK IIKGNSMFDT SAITGESVLK SIKIGERVLS
     GVINKKSVVT IEVEKLMKDS TVSKILDMVE NATSKKSKTE NFISVFAKYY TPIVVSLALL
     LAIAPTLILG EPFYKWAYRG LVFLVVSCPC ALVLSIPLTY FSGIGISSKN GILVKGSNYL
     EALRKVNIVV LDKTGTITKG TFEVSNVVLG DDITEKEIFE YARIAESRSI HPIATSIVKY
     ASNILDIDEV VDEANMTEYE EISSHGVRTV YKGKEILAGN YRLMQKFGIS YSESKSSSTK
     VHVAADRLYL GCIEISDEIK AGIFEAIDEL KKIGIERVIM LTGDTERVAS EVSHIAGFDE
     YHANLLPVDK VNILEQIIES NIGKGNVAFI GDGINDAPVI ARSDVGISMG GMGSDSAIEA
     SDIVFMTDEI SKLPIAIRIA KFTSKISWQN IFLAMGLKII VLIMSVFGLA NMWLAIFADV
     GVAVLAVLNS LRVLKRNYR
//
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