ID I7IYL9_9LACO Unreviewed; 642 AA.
AC I7IYL9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN ORFNames=BN53_00375 {ECO:0000313|EMBL:CCI84577.1};
OS Lactobacillus pasteurii DSM 23907 = CRBIP 24.76.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423790 {ECO:0000313|EMBL:CCI84577.1, ECO:0000313|Proteomes:UP000009311};
RN [1] {ECO:0000313|EMBL:CCI84577.1, ECO:0000313|Proteomes:UP000009311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.76T {ECO:0000313|Proteomes:UP000009311};
RA Cousin S., Bouchier C., Loux V., Ma L., Creno S., Bizet C., Clermont D.;
RT "Draft Genome Sequence of Lactobacillus pasteurii CRBIP 24.76T.";
RL Submitted (JUN-2012) 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:CCI84577.1}.
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DR EMBL; CAKD01000006; CCI84577.1; -; Genomic_DNA.
DR RefSeq; WP_009559130.1; NZ_CAKD01000006.1.
DR AlphaFoldDB; I7IYL9; -.
DR STRING; 1423790.BN53_00375; -.
DR PATRIC; fig|1423790.3.peg.726; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000009311; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:RHEA.
DR CDD; cd02079; P-type_ATPase_HM; 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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 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 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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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 Hydrolase {ECO:0000313|EMBL:CCI84577.1};
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:UP000009311};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 63..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 234..252
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 258..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 592..611
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
SQ SEQUENCE 642 AA; 68876 MW; 8E3756C517FB5455 CRC64;
MQKWLMKNRN RLTAISGILI VLAFAAKWLF KSETGASGLL LAASLIGGFP ISASAWQALK
VKVISIDLLV TLAILGAFVI QEFEESAIVA FLFLFGAYLE QKTLAKTRSA IKELVEMVPE
TALRQTEDGD FEEVDLDDLD EGDILLVKTG GKIPVDGEVV YGSGTANEAS ITGESMPLGK
KPGDPVYAGT ILENGTIRIK AEKVGDETTF GKIIELVEEA QDSKSQAERL IDRFSKYYTP
VVLLLAIIVG LISQDLELAV TILVLGCPGA LVIGVPVSNV AGIGNGAKQG ILFKGSEVIT
KFSKVDTIMF DKTGTLTYGD PRVSQVKKYG QGQLAEQLLV SVEKESAHPL AKAITGYYKD
LEAKEVESSQ VLQGGGIVAQ VAGRQVLVGN RYLLDQYHVP VTKEMEKNLE ELASVGNSLV
LVAVNGQLEL ALGLKDEIRA GVKEDLAALK KLGVKNLLLL SGDNQKTVDL VAEELGLTEA
YGQLLPEDKA EFVKRRQAAG EIVAFVGDGI NDSPSLARAD IGIAMGSGTD VAIETSNVVL
MNGSFDRIPR ALALAKATRR NMIENITIAL AVVAVLLVSV LASSWMNMAI GMFVHEGSIL
VVILNAMRLL AYRSKLQKSR KLIENNFSQA EGPYTKGIKS IQ
//
