ID A0A0A2TTF1_9BACI Unreviewed; 792 AA.
AC A0A0A2TTF1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN ORFNames=N782_11770 {ECO:0000313|EMBL:KGP72550.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP72550.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP72550.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP72550.1,
RC ECO:0000313|Proteomes:UP000030147};
RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT "High quality draft genome sequence of the moderately halophilic bacterium
RT Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT genomes.";
RL Stand. Genomic Sci. 10:93-93(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001390};
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:KGP72550.1}.
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DR EMBL; AVBF01000028; KGP72550.1; -; Genomic_DNA.
DR RefSeq; WP_036819664.1; NZ_AVBF01000028.1.
DR AlphaFoldDB; A0A0A2TTF1; -.
DR STRING; 1385514.N782_11770; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000030147; 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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; IPR006122; HMA_Cu_ion-bd.
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; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030147};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 406..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 440..457
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 744..761
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 3..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 70..136
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 792 AA; 85096 MW; 9AFEFF6481E560D3 CRC64;
MSKDVKIGVT GMTCAACSTR IEKVLNKMDG IEAEVNLAME NAHIHYDEEQ VSASDITAKI
EKLGYGVQTD RIELDVYGMT CAACSTRIEK VLNKMEGIQQ ASVNLTNETA QIDYQPGMVD
LDQMINKIQK LGYDAEQRAD REEKSSQKEK ELKRKQIKLG ISALLSLPLL YTMIGHLAGL
PVPALLMNPW VQMAFATPIQ FVIGWQFYEG AYKNLKNKTA NMDVLVALGT SAAYFYSLAE
AIQTLFKEDF EPHLYFETSA ILITLILLGK YFEAIAKGRT TQAISSLLNL QAKEATVVRN
GEEQQVPVDQ VQVGDTIIVR PGEKVPVDGE VTKGNSSVDE SMITGESIPV EKVAGEQVIG
STINKNGTIY MEAKKVGKDT ALANIVKVVE EAQGSKAPIQ RMADVISGYF VPIVVGIALV
TFVIWITIVS PGNLATSLEA TIAVLVIACP CALGLATPTS IMVGTGKAAE QGILFKGGEY
LEATHKIDTM VFDKTGTITK GEPEVTDFEG NTSILSYVGS AEKSSEHPLA QAIVSYVQDQ
GVSMSEPSNF EAIPGHGIQA TVDGSELLIG TRRLLSQHNV EYSKYEAIME AWEQEGKTAM
LISVDGNLEG IIAVADTVKE TALQALGQLR DQGIELVMLT GDNERTANAI AKQVGIDRVF
AEVIPEQKAD KIKELQAQEK RVAMVGDGIN DAPALATADI GIAIGTGTDV AIEAADVTIL
AGDLSLLPKA IQLSGMTMKN IRQNLFWALA YNSAGIPVAA VGLLAPWIAG AAMAFSSVSV
VSNSLRLKRV KL
//
