ID J7TXE8_STRSL Unreviewed; 695 AA.
AC J7TXE8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN ORFNames=RSSL_01524 {ECO:0000313|EMBL:EJO16758.1};
OS Streptococcus salivarius K12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1200793 {ECO:0000313|EMBL:EJO16758.1, ECO:0000313|Proteomes:UP000006983};
RN [1] {ECO:0000313|EMBL:EJO16758.1, ECO:0000313|Proteomes:UP000006983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Streptococcus salivarius K12
RC {ECO:0000313|Proteomes:UP000006983};
RX PubMed=23045482; DOI=10.1128/JB.01268-12;
RA Barretto C., Alvarez-Martin P., Foata F., Renault P., Berger B.;
RT "Genome Sequence of the Lantibiotic Bacteriocin Producer Streptococcus
RT salivarius Strain K12.";
RL J. Bacteriol. 194:5959-5960(2012).
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:EJO16758.1}.
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DR EMBL; ALIF01000001; EJO16758.1; -; Genomic_DNA.
DR RefSeq; WP_002890512.1; NZ_ALIF01000001.1.
DR AlphaFoldDB; J7TXE8; -.
DR PATRIC; fig|1200793.3.peg.648; -.
DR Proteomes; UP000006983; 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; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 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; 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 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; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 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:EJO16758.1};
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 310..331
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 337..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 643..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 667..686
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..67
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 695 AA; 76038 MW; A3E03EF103E83349 CRC64;
MKKEYELRGI DCGNCAAKIE RAVNQLEQVE SATVNLIAQK LILETKSEDG IDKEIIDLVD
AIEPGIEVIS EKKEEALPEK RDWAKELLLA VMILFAFGFF LPEEYFWIRL VYYLTLYIII
GHKVLIKMVQ NIQRGNLFDE NFLMSIATLG AFLLGEFPEA VAVMLFYQIG EYFQDKATSQ
SRQSIARLMD IRSDKAWRLE GGETVQVDPE TVRVADHILV KPGEKVPLDG LVREGRSILD
TSALTGESLP REIGVGEDIT SGVINLTSPL VIEVSKTFSQ STVNKILELV ENASNKKAET
ERMITRFSRV YTPVVVGIAF LLASLPPLLG LGEWSTWLYR ALTFLVISCP CALAVSVPMS
FFGGLGGASK LGVLVKGGNY LEALAKLDTV VFDKTGTITK GIFAVDTVVN AEGVEDDILY
LAAHLESYSN HPIANSIRTA YGQEVDENRV SQITELPGQG MSGRVDGRQL YLGNARLMEV
QGIAYPAIDS TGTVLYLAED SHFLGYFLIT DQVKETSIEA LKDLQAVGIK KTVLLSGDRQ
AVVDEFAQQF AFNDAFGDCL PQDKVSTFEE ILTQSQQAVA FVGDGVNDAP VLARADVGIA
MGGLGSDAAI ESADVVLMDD DLGKLPQVIR LAKKTVRIAQ QNMTLAIVVK LIFLVLSGLG
ISNMWEAIFA DVGVTLLAVW NALRVLRIDT STLSK
//
