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Database: UniProt
Entry: A0A239Y1Z4_9SPHI
LinkDB: A0A239Y1Z4_9SPHI
Original site: A0A239Y1Z4_9SPHI 
ID   A0A239Y1Z4_9SPHI        Unreviewed;       965 AA.
AC   A0A239Y1Z4;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Cu2+-exporting ATPase {ECO:0000313|EMBL:SDL25801.1};
GN   ORFNames=SAMN05192578_102122 {ECO:0000313|EMBL:SDL25801.1};
OS   Sphingobacterium mizutaii.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1010 {ECO:0000313|EMBL:SDL25801.1, ECO:0000313|Proteomes:UP000199201};
RN   [1] {ECO:0000313|EMBL:SDL25801.1, ECO:0000313|Proteomes:UP000199201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11724 {ECO:0000313|EMBL:SDL25801.1,
RC   ECO:0000313|Proteomes:UP000199201};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNGK01000002; SDL25801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239Y1Z4; -.
DR   STRING; 1010.SAMN05192578_102122; -.
DR   Proteomes; UP000199201; 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: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; IPR045800; HMBD.
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; 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; PF19335; HMBD; 3.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
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; PS01229; COF_2; 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:ARBA00022796};
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   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:ARBA00022796}.
FT   TRANSMEM        307..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        341..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        372..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        410..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        567..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        599..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        910..929
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        935..957
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          7..71
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          83..147
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   965 AA;  105267 MW;  46F4BED051C89583 CRC64;
     MVNSTMKNHT YKVTGMTCNG CRTNVEKKLN EIPGVNAQVS LEKAEAHLQT DEPVHISNLQ
     EKLNELGGHY QIHNNESENV GPTDKTFTVT GMTCNGCRTN VEKKLNEIPT VKASVNLEKG
     EAQILSDSPI PTEELQNKLD ELGGHYQIHE KGAHEHKHHH AHEPELSESG QYICPMFCEG
     KDKIYHEPGR CPVCNMHLRP IEKVDFNAPS HHHQAQPTVN ASNAGKYYCP MMCEGDKVYD
     KFGSCPVCGM NLEKIPDTTL KVEYTCPMHP EIVQDHPGDC PICGMELVPN QVTEEDDQHY
     RDLLKKFWIS VACTLPVFIL SMGDMLPGQP ISQVIPYKVN AWLQLILTLP VVFYTCWMFF
     QRAWTSFKTW NLNMFSLIGL GAAAAFIFSL LAFFFPQIFP EELKGHHGEV HLYFESVVVI
     LTLVLLGQVM EAKAHSKTNT AIKELIKLSP AEAILVENGK ERKISIHDVK VGNILRVRAG
     DKVPVDGIVT EGNTSIDEAM ITGEPIPVEK SKDDQVIGGT INGNHEILIK AEKVGSETLL
     AQIIQLVNNA SRSQPPIQKL TDKVSKIFVP AVIAIAILTF ILWNVSAVPN STAMAFSNML
     AVLIVACPCA LGLATPMSVM VGIGKGAKNG ILIKNSEALE KLEKANVLVV DKTGTITEGK
     PSVSAVTSEN DKFSENDILQ IAASVNKNST HPLAQAMTDK AKENGLQLLD VAQFENISGK
     GVKGHIFHMT ALLGTPRLME EQKIEVSKDQ LQKIEELQKK GNSVSVLAID GKVAGLVAAF
     DALKKSSIDV IKRFKEEGVE VYMFTGDNQN TADIVAKEAG IEHAKGSLLP EDKLNGIKEL
     QQAGKKVIMV GDGINDAPAL TQADVGIAMG TGTDVAIQSS EITLIKGDLI GVHKAFKLSK
     SMLRNIKQNL LFAFLYNVIG IPIAAGILYP SFGILMSPMI AAAAMSLSSV SVIVNSLRLN
     AVKLD
//
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