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Database: UniProt
Entry: A0A1I4HP77_9FIRM
LinkDB: A0A1I4HP77_9FIRM
Original site: A0A1I4HP77_9FIRM 
ID   A0A1I4HP77_9FIRM        Unreviewed;       714 AA.
AC   A0A1I4HP77;
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=SAMN02983006_01123 {ECO:0000313|EMBL:SFL43361.1};
OS   Halanaerobium salsuginis.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=29563 {ECO:0000313|EMBL:SFL43361.1, ECO:0000313|Proteomes:UP000199006};
RN   [1] {ECO:0000313|EMBL:SFL43361.1, ECO:0000313|Proteomes:UP000199006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51327 {ECO:0000313|EMBL:SFL43361.1,
RC   ECO:0000313|Proteomes:UP000199006};
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; FOTI01000012; SFL43361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4HP77; -.
DR   STRING; 29563.SAMN02983006_01123; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000199006; 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   CDD; cd07548; P-type_ATPase-Cd_Zn_Co_like; 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; 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; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
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   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:UP000199006};
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        106..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        133..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        335..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        366..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        664..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        691..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          11..75
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   714 AA;  77382 MW;  D8F485398EFFBDD0 CRC64;
     MTTGLSEKAK VKEEYELEGL NCSNCALKIE NKVKELDGLE EVELNFATST LKLVAPETEI
     ASMEHKLQSI SDRIEPGVKV KKRGDESPEK DSAASKFSFI WAKKEIFIGA IIFALIMLFT
     KTNLFAVQLP TPVVIISFLT AYILIGWPVL KAAFFNIGQG QIFDENFLMV IATFGAFAIQ
     EYPEAVAVML FYMIGELFQE RAVNSSRRSI KELMDIKADY ANLFVAGQTK QVKPEDLEID
     DLIIIKAGEK VPVDGEVISG NSALETSALT GESIPRDVEP GSAVLSGMIN LNSLLKVKVK
     RPYKDSTVKK ILDLVENASS KKANTEKFIT KFARYYTPAV VAAAAAVSVL PPVFGLGTFS
     TWFYRALIFL VVSCPCALVV SIPLGFFGGI GLASRNGILI KGGNYLEALN SVTGVVFDKT
     GTLTEGNFAV REIKSLSQYS QAELLSLAAE VEQFSNHPIA TSILEKSQKY QKHDPESNYQ
     EISGGGIKAI LAGREILAGN ERLMKNNNIK FEKVDQPGTV VYLAENGSYL GYILISDKLK
     ADAEQAISGL KKLGLSNIAM LTGDNKNAAH QIAEQLGLDS YYANLLPDQK VAKVEELLAN
     SQGKLAFVGD GINDAPVLAR SDLGIAMGGL GSDAAIEAAD IVLMTDEPNK LVTALEIAAE
     TKKLIWQNIV MALGIKAIVM ILSILGMASM WLAVFADVGV ALLAVFNVMR ILKR
//
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