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Database: UniProt
Entry: A0A174HNQ0_9CLOT
LinkDB: A0A174HNQ0_9CLOT
Original site: A0A174HNQ0_9CLOT 
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
//
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