ID A0A174GY36_9FIRM Unreviewed; 860 AA.
AC A0A174GY36;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
DE AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN Name=cadA {ECO:0000313|EMBL:CUO65709.1};
GN ORFNames=DWY46_09775 {ECO:0000313|EMBL:RGR49243.1}, DXB38_16665
GN {ECO:0000313|EMBL:RGN83153.1}, ERS852394_02693
GN {ECO:0000313|EMBL:CUO65709.1};
OS Blautia obeum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=40520 {ECO:0000313|EMBL:CUO65709.1, ECO:0000313|Proteomes:UP000095409};
RN [1] {ECO:0000313|EMBL:CUO65709.1, ECO:0000313|Proteomes:UP000095409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608837 {ECO:0000313|EMBL:CUO65709.1,
RC ECO:0000313|Proteomes:UP000095409};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000261105, ECO:0000313|Proteomes:UP000285839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF25-21 {ECO:0000313|EMBL:RGR49243.1,
RC ECO:0000313|Proteomes:UP000285839}, and OM03-6
RC {ECO:0000313|EMBL:RGN83153.1, ECO:0000313|Proteomes:UP000261105};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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; CYZD01000017; CUO65709.1; -; Genomic_DNA.
DR EMBL; QSUZ01000048; RGN83153.1; -; Genomic_DNA.
DR EMBL; QRUH01000006; RGR49243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A174GY36; -.
DR Proteomes; UP000095409; Unassembled WGS sequence.
DR Proteomes; UP000261105; Unassembled WGS sequence.
DR Proteomes; UP000285839; 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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR CDD; cd00371; HMA; 3.
DR CDD; cd07548; P-type_ATPase-Cd_Zn_Co_like; 1.
DR Gene3D; 3.30.70.100; -; 3.
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; IPR006122; HMA_Cu_ion-bd.
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 NCBIfam; TIGR00003; copper ion binding protein; 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; 3.
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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 3.
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 Copper {ECO:0000256|ARBA:ARBA00023008};
KW Hydrolase {ECO:0000313|EMBL:CUO65709.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
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:UP000095409};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 279..298
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 511..537
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 815..834
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 77..145
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 154..222
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 218..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 92752 MW; 467E8040E34A3DBE CRC64;
MERIFLLKGL DCPNCSAKIE KEVGDLENVN SSSVNLMKQT LTIQTETFDN SIVEQIETIV
HSHEPDVEVS EKKESYTTKT YLLKGLDCPN CSAKIEKEVG DLEDVSSSVV NLMKQTLTIS
VKTSASGKIQ DEVATIVHSH EPDVKVSEQT DSYVTKKYLL KGLDCPNCSA KIEKEVGELE
GVALSEVNLM KQTLTVSMDH NKAASMLDMV TTIVHSHEPD VEVSEQKADT SVAPDKKEKT
PVYSDDDKKL TIRLISGAVI YAVGMGLTLF GHVSLPVELG VLIVAYIILG WDVVWQAVKN
ITRGQIFDEH FLMSLSTIGA FAIGEYPEAV AVMLFYQVGE FFQSLAVKRS RKSISDLMDI
RPDSATVRRN GELVVVAPET VSIGELIVVK PGEKIPLDGI VTEGESMLDT RALTGESVPR
SIRKGEEALS GCVNQSGVLT IKVTKSFGES TVTKIIDLVE NASSRKAPTE NFITTFARYY
TPIVVGMAAI LAIIPPVILG GGWSEWLRRG FVFLIVSCPC ALVISIPLTF FGGIGAASKR
GVLVKGSNYL EALNKVSVVV FDKTGTLTKG VFKVVDITVE FGFTKEQVLE YAAQAESYSN
HPIAKSIQEA FGKTIDQSVL SGYEEISGHG IRVLIGGKRV LAGNSKLMDS EKVSYAACQS
AGTKVYIAVD GRYAGCIVIA DEVKDDSQNA IASLKKIGVE KTVMLTGDDE KIGKAVAEQL
GLDEYYAQLL PDQKVEKLEY LDQHKTKGSK LAFVGDGIND APVLARADVG IAMGGLGSDA
AIEAADVVLM TDEPSKLVDA IDVAKATKRI VMQNIIIALG IKSVFLILGA LGIAGMWEAV
FGDVGVTIIA VLNAMRILKK
//
