ID A0A1T5M950_9CLOT Unreviewed; 808 AA.
AC A0A1T5M950;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN ORFNames=SAMN02194393_04210 {ECO:0000313|EMBL:SKC84772.1};
OS Maledivibacter halophilus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Maledivibacter.
OX NCBI_TaxID=36842 {ECO:0000313|EMBL:SKC84772.1, ECO:0000313|Proteomes:UP000190285};
RN [1] {ECO:0000313|EMBL:SKC84772.1, ECO:0000313|Proteomes:UP000190285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:SKC84772.1,
RC ECO:0000313|Proteomes:UP000190285};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUZT01000012; SKC84772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5M950; -.
DR STRING; 36842.SAMN02194393_04210; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000190285; 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 HMA2; 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; 1.
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 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:UP000190285};
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 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 455..476
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 760..779
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 785..803
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 5..67
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 84..152
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 162..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 88233 MW; DBAA0CCE887BA321 CRC64;
MLKKAKIELM LEGLDCANCA GKIERKVSEL KEVIMVSLNF VTKILTIEID SIDEIEAVIL
ETKNIVKRYE PHVVVKEKII DKASKKVLVL MGLVCASCSA KIEGKIKDLK GVQNAYIDFA
TGKLIIEGNK KDLNSITKQA IEIVKKIEPD VDVVEENKKD IQRNSHNHDN DNCDGACQGH
VHNHTHEHNH GEGKNKRELI RLGIGAALFL TAIIFKFSYP IEFIIYFASY ILVGGEVLLR
AVKNIIRGQV FDENFLMAIA TVGAFVIGEF PEGVGVMLFY QVGEFMQGLA VNRSRKSIAD
LMDIRPDYAN LKIGNEIERV SPENVSVEDI IVVKPGEKIP LDGIITLGNS TVDTSALTGE
SVPREVETGD EVLGGFINKR GLLNIKVTKE FGESTVSKIL DMVQNASSKK APTENFITKF
ARYYTPVVVF SALALAVIPP LIIDGATFSE WIYRALIFLV VSCPCALVIS IPLGFFGGIG
GASKNGILVK GGNYLEALNN VDTVVFDKTG TLTKGVFKVT EIKTSNNISK EELLEFAALA
ESYSNHPIAT SILKEYGKEI DKEDIQSYNE ISGFGITAVV KGKEILAGND KLMKQNNIEF
TSIDIPGTII HIVIEREYAG YIIISDEIKE DSKEAIIGLK AIGIRNTVML TGDNKNVAAK
VADKLGLDKV YSELLPHHKV EKIEMLERQK KSKDKLIFVG DGINDAPVLA RVDVGVAMGA
LGSDAAIEAA DVVLMTDEPS KLVSAIKIAK RTKRIVMQNI IFSLAVKGGV LLLGAIGYAT
MWEAVFADVG VALIAVLNSM RVLNVKNI
//
