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Database: UniProt
Entry: C0EHA3_9FIRM
LinkDB: C0EHA3_9FIRM
Original site: C0EHA3_9FIRM 
ID   C0EHA3_9FIRM            Unreviewed;       725 AA.
AC   C0EHA3;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 80.
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:EEG29190.1};
GN   ORFNames=CLOSTMETH_03303 {ECO:0000313|EMBL:EEG29190.1};
OS   [Clostridium] methylpentosum DSM 5476.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillospiraceae incertae sedis.
OX   NCBI_TaxID=537013 {ECO:0000313|EMBL:EEG29190.1, ECO:0000313|Proteomes:UP000003340};
RN   [1] {ECO:0000313|EMBL:EEG29190.1, ECO:0000313|Proteomes:UP000003340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG29190.1,
RC   ECO:0000313|Proteomes:UP000003340};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG29190.1, ECO:0000313|Proteomes:UP000003340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG29190.1,
RC   ECO:0000313|Proteomes:UP000003340};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium methylpentosum (DSM 5476).";
RL   Submitted (FEB-2009) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEG29190.1}.
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DR   EMBL; ACEC01000115; EEG29190.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0EHA3; -.
DR   STRING; 537013.CLOSTMETH_03303; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_6_2_9; -.
DR   Proteomes; UP000003340; 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; IPR017969; Heavy-metal-associated_CS.
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   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; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
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; PS01047; HMA_1; 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   Hydrolase {ECO:0000313|EMBL:EEG29190.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003340};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          2..65
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   725 AA;  77346 MW;  68851C257EEB488E CRC64;
     MVKYKYALDG LNCANCAAKI EAQVGQMEGV HTATVDFVGK SLTIQTDQDI AAFEKKAAPL
     IRSIDGNVKL ISASQQGQQK SKSNFHLPIF TAVASILLFV AGMITEKAFH LEVAGAICFG
     GAALLAGYQV FLSGFKALAR FKLDENTLMT IAVIAAFCLG EFSEAAMVAI LFHLGEMLEE
     KAVNRSRRDI EHLAEIRPDT ARLISGEDHC DCEEHEQEHQ HDHTHGVEHE HCDCCEHHHE
     EGGERVVPAE QVQIGDVISV HPYERIPLDG KILTGNSSLD SSALTGESMP LEAEPGTEVL
     SGMMNGQGLI TVEVTNDFSN SAASRIIDMV ESSAARKGHA EKLITRFAAI YTPIVIVLAV
     LLMAIPPLLG LGAFTTWFYR ALIFLVASCP CALVISVPLG FFAGIGAQSK NGVLVKGGKY
     VEVLSHPDAV VFDKTGTLTS GKLSVTEIVS TGSLSQQELL QLAASAEQYS SHPAAQAVLA
     ANTGELLPAA DPNEIAGQGV VARVNDRQIL CGRQPLMDRY GVETKGHKAS IFIAVDGKLE
     GMLQLADTVK PDSTEAVRRL KELGVKRVVM LTGDNEQSAA KAAEQCGITE YHAGLLPENK
     VSLMEQIRKE SGRTIFVGDG INDAPVLAAS DCGVAMGLGT DAAIEASDVV LTVDRPSKLA
     DAVSLSARSM RVIRFNIAFA LIVKAAVLVL AATGFAPMWL AVFADVGVSI LSVINATRIL
     RFQLK
//
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