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Database: UniProt
Entry: A0A1Z5IA82_9LACO
LinkDB: A0A1Z5IA82_9LACO
Original site: A0A1Z5IA82_9LACO 
ID   A0A1Z5IA82_9LACO        Unreviewed;       628 AA.
AC   A0A1Z5IA82;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE            EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN   ORFNames=IWT30_00593 {ECO:0000313|EMBL:GAW98634.1};
OS   Secundilactobacillus mixtipabuli.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Secundilactobacillus.
OX   NCBI_TaxID=1435342 {ECO:0000313|EMBL:GAW98634.1, ECO:0000313|Proteomes:UP000198374};
RN   [1] {ECO:0000313|EMBL:GAW98634.1, ECO:0000313|Proteomes:UP000198374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IWT30 {ECO:0000313|EMBL:GAW98634.1,
RC   ECO:0000313|Proteomes:UP000198374};
RA   Tohno M., Tanizawa Y., Arita M.;
RT   "Draft genome sequences of new species of the genus Lactobacillus isolated
RT   from orchardgrass silage.";
RL   Submitted (NOV-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}.
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:GAW98634.1}.
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DR   EMBL; BCMF01000003; GAW98634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5IA82; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000198374; 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   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; 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; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
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   PROSITE; PS00154; ATPASE_E1_E2; 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:UP000198374};
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        24..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        47..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        78..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        247..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        278..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        584..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   628 AA;  67268 MW;  D852C105D1D9AC95 CRC64;
     MKLATVPART RQTFRGLLAH KNDLLLISSS TIILLIAVSL PVSALKIILY LASYMIISYP
     IIWQSLTNII HGNFFDETFL MTVATVGAIA LGDYPEAIAV MLFYQIGDLF EDVAVQQSRQ
     SISALLKLKS TTATVVTNTG EHVVDPEQVI PGQTIRVKPG ERVALDGQLK RGKTSLDTSA
     LTGESLPRDV QSGDLVLSGT INLTDVIDIQ VTKPYQESTI ARILDLVQNA AQKKTVTEKF
     ITRFAKIYTP VVVGFAVVLA LFPPLLQFGS WATWINRALV FLVISCPCAL VISVPLSFFG
     GIGAASRHGI LVKGSNFLEV LTRVTTVAFD KTGTLTQGHF TVNKISPQVP LSSHQLLGIA
     AAAEQHSNHP IARSITSAFT ADLSHFQVHD ITETAGHGIK AVVDGQQIIV GNAKTMAENQ
     VTMPAAHAAC TTVYVAINQQ FAGSIEVADQ PKPDSKGAIR TLNQLDIAQT VLLTGDNQAV
     ANQISCELGL STVKADLLPT QKVTEMEKLT HSAHQTNHRV AFVGDGINDT PVLARADVGI
     AMGGLGADAA IEAADVVIMD DKPSKVATII QIAKATKRIV WENITFALSI KVIFLILGAL
     GMIGMWEAVF ADVGVTMIAI LNALRLQH
//
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