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Database: UniProt
Entry: A0A1M6LCM0_9FIRM
LinkDB: A0A1M6LCM0_9FIRM
Original site: A0A1M6LCM0_9FIRM 
ID   A0A1M6LCM0_9FIRM        Unreviewed;       631 AA.
AC   A0A1M6LCM0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE            EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN   ORFNames=SAMN02745691_02376 {ECO:0000313|EMBL:SHJ68927.1};
OS   Parasporobacterium paucivorans DSM 15970.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Parasporobacterium.
OX   NCBI_TaxID=1122934 {ECO:0000313|EMBL:SHJ68927.1, ECO:0000313|Proteomes:UP000184342};
RN   [1] {ECO:0000313|EMBL:SHJ68927.1, ECO:0000313|Proteomes:UP000184342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15970 {ECO:0000313|EMBL:SHJ68927.1,
RC   ECO:0000313|Proteomes:UP000184342};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQYT01000034; SHJ68927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6LCM0; -.
DR   STRING; 1122934.SAMN02745691_02376; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000184342; 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; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
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; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000184342};
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        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        41..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        242..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        269..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        587..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        612..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   631 AA;  68200 MW;  9FE2F4CA858A3938 CRC64;
     MKFNRELSKI IITAVLFILV QLIPFEKISL LQKIGNGDAE LFSYLIIYII IGGAVLKEAA
     SNIRQGEIFD ENFLMSIATV GAFFIGEYPE AVAVMLFYQV GEFFQSYAVD KSRKSVSALM
     DIRPDSAYLK QKDGSVVKVH PEDVNVGQVI VVRPGEKVPL DGTVISGAGD LDVRALTGES
     LPREAVEGDA IISGSVNING LFEIIVEKKF TESTVSKILE LVENAGNKKA VAENFITKFA
     RIYTPFVVFA AVVIAVAPPL FAGGVWSDWI YRALTFLVIS CPCAFVISVP MSFFGGIGGA
     SRRGILIKGS NYIETLAKCN TIVFDKTGTL TKGVFRLEKI NALGVREEEL LETAAIAEYY
     SNHPIARSIM DAFQKSNPER YGWVKERIAG ATARELPGFG MQVSLSAEGG MSEIIAGNKR
     LFRKEGIEIH EEKEVGSVVY VAKDGVFLGS LEVSDEIRSD AVKGINLLKK YGIRNTVMLT
     GDKESAAQKI GKQLGIDRIF SELLPMDKVS KLEEIMGQSD SPVVYVGDGI NDAPVLARAD
     VGIAMGGLGS DAAIEAADIV IMDDKVGGVS EAIRISRKTL RIVNQNVVFA FGVKLIVLVL
     AAMGIADMWP AVFADVGVAT IAILNALRAL R
//
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