ID A0A1M5SE98_9FIRM Unreviewed; 714 AA.
AC A0A1M5SE98;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN ORFNames=SAMN04488530_1403 {ECO:0000313|EMBL:SHH36799.1};
OS Asaccharospora irregularis DSM 2635.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Asaccharospora.
OX NCBI_TaxID=1121321 {ECO:0000313|EMBL:SHH36799.1, ECO:0000313|Proteomes:UP000243255};
RN [1] {ECO:0000313|Proteomes:UP000243255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2635 {ECO:0000313|Proteomes:UP000243255};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQWX01000040; SHH36799.1; -; Genomic_DNA.
DR RefSeq; WP_073127362.1; NZ_FQWX01000040.1.
DR AlphaFoldDB; A0A1M5SE98; -.
DR STRING; 1121321.SAMN04488530_1403; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000243255; 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:UP000243255};
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 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 334..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 665..685
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 691..710
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 7..76
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 714 AA; 77618 MW; 464C5E2475983042 CRC64;
MAGSGLIKKE LILNGLNCAH CAQVINEKVS KLEGIEECNL NFINKKLTVN INESKNEEEI
ISTIINIIDS TEPGLDIKII SDSEDDKEDH DHGHDHSHNH DVSKKDLIKL IIGSIVYIFG
IYQIFTGIES KFADLLFIVA YIVVGGEVLT KAVKNIFRGQ VFDENFLMTI ATIGALAIGE
LPEAVGVMLF YQIGEFLQGV AVGKSRKSIS ELMDIRPDYA NLKTGSEISV VSPKEVSIGE
VIVIKPGEKV PLDGIVVEGN SMLDTSALTG ESVLKEISVG DEVLSGFINK NALLSVKVTK
GFGESTVSKI LELVENANNK KSKTENFITK FSKYYTPVVV IAALLIAVVP PIVIPGALFS
DWLYRGLIFL VVSCPCALVL SIPLSFFSGI GFASKNGVLI KGSNYLEALR DVDTVVFDKT
GTLTKGVFGV TKVNPVGISE EQLIEYAAIA EVNSNHPIAQ SIIKHYNKKI DLDKIEKYEE
IAAHGIKVLY NGDFILAGNE KLMKQENVLF DRAEEIGTVI YISVNKTYRG HIVISDEIKP
DSKEAIKSLR SIGIKKVVML TGDNEKVANN VAKELGIDKV YSNLLPNEKV DKIEELYKGR
TEKEKIAFVG DGINDAPVLA RVDVGIAMGG LGSDAAIEAA DVVLMTDEPK MISKTMDIAN
KVNKIVWQNI SFALGVKIIV MILGAGGVAT MWEAIFADVG VALIAVLNSM RVMR
//
