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Database: UniProt
Entry: M0P0B7_9EURY
LinkDB: M0P0B7_9EURY
Original site: M0P0B7_9EURY 
ID   M0P0B7_9EURY            Unreviewed;       898 AA.
AC   M0P0B7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Copper-transporting ATPase {ECO:0000313|EMBL:EMA63283.1};
GN   ORFNames=C468_10111 {ECO:0000313|EMBL:EMA63283.1};
OS   Halorubrum kocurii JCM 14978.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1230456 {ECO:0000313|EMBL:EMA63283.1, ECO:0000313|Proteomes:UP000011546};
RN   [1] {ECO:0000313|EMBL:EMA63283.1, ECO:0000313|Proteomes:UP000011546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14978 {ECO:0000313|EMBL:EMA63283.1,
RC   ECO:0000313|Proteomes:UP000011546};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA63283.1}.
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DR   EMBL; AOJH01000062; EMA63283.1; -; Genomic_DNA.
DR   RefSeq; WP_008848729.1; NZ_AOJH01000062.1.
DR   AlphaFoldDB; M0P0B7; -.
DR   STRING; 1230456.C468_10111; -.
DR   PATRIC; fig|1230456.3.peg.2002; -.
DR   OrthoDB; 8588at2157; -.
DR   Proteomes; UP000011546; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0005507; F:copper ion binding; IEA:InterPro.
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; 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; 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; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   NCBIfam; TIGR00003; copper ion binding protein; 1.
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; 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   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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022796};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT   TRANSMEM        179..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        429..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        862..882
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..70
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          72..138
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          136..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   898 AA;  93527 MW;  5362CFE7F3B17091 CRC64;
     MPTRTAHLNV TGMSCANCSA SIEDALDDLD GVASANANYA TDEGSVEYDP EEVSLGELFD
     AIESAGYGAV SQTVSVAITD MSCANCAEAN ADALESTPGV IEATVNYATD EAQVRYNPAD
     ASLEDLYDAI ESAGYSPVRE GSGSGGDGEG SGAGAGAGDS GQDARDAARE EEIRKQLRLT
     LFGAVLATPL LAFMTDHLLF GGEIFPETVF GVSFGWVQFL LATPVQIVLG RPFYRNSYKA
     LVTNGRANMD VLIALGSTTA YVYSVASLSG AIAGGLYFDT AAFILVFITL GNFLEARSKG
     QAGEALRKLL EMEADTATLV DEDGTEREVP LDEVAVGDRM KVRPGEQIPT DGVVVDGQSA
     VDESMVTGES VPVEKESGDE VVGSTINENG VLVVEATKVG SDTALQQIVR TVKEAQSRQP
     EIQNLADRIS AYFVPAVIVN AVLWATVWFL FPEALAGFVD GLPLWGLVAG GPGAAGGGVS
     VFEFAIIVFA SAVLIACPCA LGLATPAATM VGTTIGAGHG VLFKGGDVLE RAKDVDTVVF
     DKTGTLTEGE MELTDVIAFD REGNPIPDGG TASRADSGEG DLAASDTDRL GENDVLRLAA
     IAERGSEHPL ARAIVDGAEE RGLDVSEPEA FENVPGHGVR ATVAPDHLDG GSEVLVGNRK
     LLRDNGIDPA PAAEEMERLE SEGKTAMLVA RVPAGTNDGR LAGIVADADT VKPSAADAVA
     ALRDRGVDVM MITGDNERTA RAVAERVGID PENVRAGVLP EDKSDAVEAI QADGRQAMMV
     GDGVNDAPAL AVAYVGTAIG SGTDVAIEAA DVTLMRDDPL DVVKAIRISD ATLQKIKQNL
     VWALGYNTAM IPLASLGLLQ PVLAAGAMAF SSVSVLTNSL LFRRYEPDRD YELLGRLR
//
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