ID A0A174HNQ0_9CLOT Unreviewed; 830 AA.
AC A0A174HNQ0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:CUO76582.1};
GN ORFNames=ERS852471_02248 {ECO:0000313|EMBL:CUO76582.1};
OS Clostridium disporicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84024 {ECO:0000313|EMBL:CUO76582.1, ECO:0000313|Proteomes:UP000095594};
RN [1] {ECO:0000313|EMBL:CUO76582.1, ECO:0000313|Proteomes:UP000095594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834856 {ECO:0000313|EMBL:CUO76582.1,
RC ECO:0000313|Proteomes:UP000095594};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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; CYZX01000015; CUO76582.1; -; Genomic_DNA.
DR RefSeq; WP_055266610.1; NZ_CYZX01000015.1.
DR AlphaFoldDB; A0A174HNQ0; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000095594; 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; 2.
DR CDD; cd07548; P-type_ATPase-Cd_Zn_Co_like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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 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 HMA4-RELATED; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
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:CUO76582.1};
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:UP000095594};
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 226..242
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 248..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 482..507
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 782..804
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 810..829
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 6..71
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 115..184
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 830 AA; 90572 MW; D9D12DF59605E764 CRC64;
MDDDVKKVKL LLKGLSCANC ANKIESKVSN INGIKEATVN FATSTLIAEV FVNHNKEEII
NQIKDIVKSI EKDVIVEEVK GNIKRPARTI SRCEDGCCTI NNHSDNYTND KTVNKSNRIL
LKGLTCANCA NKIEAKVKNL DSIKYANINF ATTTLLVELN KGYKIEEAFK EINKIVKSLE
PDVEVELQET SKKGKRNRTI LSDASSSNEV VCEKEKKTTM SYVKENIFLV IGTLGFVLAV
MLESYPLIAF IFFAATYLII GKNVLITAAK NILRGEVFDE NFLMAIATLG AFAIGEYPEA
VAVMLFFEIG EAFQKYAVER SRKSISSLMN IRADYATVLE NGNEIRVDPE DVEIDEIIII
KPGERVPLDG IVVDGTSFID TSALTGESVP REITVDTEIL AGAINNTGVL KVRVTKEYGE
STVARILELV ENASNKKALT EKFITKFSKI YTPVVCLIAL LVAVVPPLIM KDQTFSVWIY
RALSLLVVSC PCALVVSVPL GIFAGIGGAS KKGVLVKGGN YLEALKDVET VVFDKTGTLT
KGVFKVTEIN TNNIDKDELL KLAAYGESNS NHPIALSIVK AYGKEINKES LINYEEISGH
GIKVNIEGNE VLLGNYKLMN KFNIKFNEVD TIGTIVHVAI NGKYKGNIVI SDEIKETSKE
AIETLKSIGI KNTVMLTGDN KVVADKVGKI IGLDQVYSEL LPADKVEQVE KLMNIKSSKG
KLVFVGDGIN DAPVLARADI GIAMGGIGSD AAIEAADVVL MKDDPKSIVD AIKAARKTNK
ILWQNIIFAL AVKTIVMILV AFGIGTMWEA VFADVGVTIL AVINSIRCLR
//