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Database: UniProt
Entry: A0A2G2K9Q0_9FLAO
LinkDB: A0A2G2K9Q0_9FLAO
Original site: A0A2G2K9Q0_9FLAO 
ID   A0A2G2K9Q0_9FLAO        Unreviewed;       829 AA.
AC   A0A2G2K9Q0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:PHS07311.1};
GN   ORFNames=COA88_09070 {ECO:0000313|EMBL:PHS07311.1};
OS   Kordia sp.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=1965332 {ECO:0000313|EMBL:PHS07311.1, ECO:0000313|Proteomes:UP000221821};
RN   [1] {ECO:0000313|Proteomes:UP000221821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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}.
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:PHS07311.1}.
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DR   EMBL; NVVR01000019; PHS07311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G2K9Q0; -.
DR   Proteomes; UP000221821; 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; 1.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 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; 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   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; 1.
DR   Pfam; PF19335; HMBD; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
DR   PRINTS; PR00942; CUATPASEI.
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; 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   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   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        175..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        238..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        273..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        433..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        458..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        775..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        800..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..66
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   829 AA;  90249 MW;  53589126F80BB9E4 CRC64;
     MKRTYHIHGM TCNGCRSHVE ETLSKVEGVS TVLVNLEKAE ATIEMKSHII LEVFQQALKD
     DSDRYSIHNI GEHKHQAKKK ESVAPQGIGT FYCPMHCEGK KTYAQKGDCP VCGMDLVEEL
     SLSPKDIQFS CPMHPEIVKD EMGNCPICGM DLIAMEPTEN DDDKTYRNLL KKMKITVLFT
     VPIFIIAMAD LIPGNPLSKI FEQQTWNWVQ LVLSIPVVFH TCWMFFERAW KSIITWNLNM
     FTLIGIGTGV AWLFSLVALL YPDVFPDQFK TEAGTVFIYF EATTVILTLV LLGQLLEARA
     HGQTSGAIKE LLKLAPTKAT LVTPKGDVVI SINEIQKGDL LRVKPGDKIP VDGKITEGNS
     NVDESMITGE PIPVDKKLND SVSSGTINGI RSFVMQAEKV GSETLLSQII QMVNKASRSR
     APIQKLADKI AKYFVPIVLL IATITFVVWR YYGPEPTMVF AFVNAIAVLI IACPCALGLA
     TPMSVMVGVG KGAQNGVLIK NAEALENLNK VDVLITDKTG TITEGKPSVE KVVNALGKYD
     DKLTEYIVSL NQYSEHPLAE AIVKFGKDKN ISPQVSNDFE AVIGKGVIGT VANTKIVIGN
     KKLMEEVGSS LSEEINKNII SEQEQGKTVS YISVNGKVEG FVCITDAIKE TSKQAINTLQ
     KLGIDVIMLT GDNKRTAKSV ADFLNLTSFQ AECLPEDKLN VIKKLQSEGK VVAMAGDGIN
     DAPALAQANI GIAMGTGTDV AIESSEVTLV KGDLLGIVKA INLGTKVMTN IKQNLFFAFI
     YNVLGVPVAA GLLYPVFGIL LSPMIAAAAM SFSSVSVIVN ALRLRNIKI
//
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