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Database: UniProt
Entry: A0A0G0UU96_9BACT
LinkDB: A0A0G0UU96_9BACT
Original site: A0A0G0UU96_9BACT 
ID   A0A0G0UU96_9BACT        Unreviewed;       916 AA.
AC   A0A0G0UU96;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 41.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:KKR92283.1};
GN   ORFNames=UU42_C0002G0097 {ECO:0000313|EMBL:KKR92283.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWA1_41_13b.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618555 {ECO:0000313|EMBL:KKR92283.1, ECO:0000313|Proteomes:UP000034676};
RN   [1] {ECO:0000313|EMBL:KKR92283.1, ECO:0000313|Proteomes:UP000034676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKR92283.1}.
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DR   EMBL; LCAO01000002; KKR92283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0UU96; -.
DR   PATRIC; fig|1618555.3.peg.375; -.
DR   Proteomes; UP000034676; 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; 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; 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   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; 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   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        223..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        292..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        329..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        481..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        509..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        828..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        857..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        887..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          2..68
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          132..198
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          110..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   916 AA;  98894 MW;  CF63FD39BA834BF6 CRC64;
     MKKVELQIKG MHCSSCEMLI KDELSSMDGI TDIVVNSKTG KASLNLKNGD ISDLMILDAI
     KNAGYQGSIV NPSPVFNSNT FTLPPEINFD AKISKDENGE LHISGKLNLS KQNEPEVLSE
     TSNENTEDQG NGRTNLLISG MHCTSCAGLI EKQLKKVQGV SEARVNFASE KASIVYDSNV
     SKLEDLVKAV EKAGYSAQPE TEELSKNQSV RQEEEIKNQW SKFVLSFLLS APMIYFMFLD
     FFKFLPGGTL LLPYIGIISF ILATPVQFYI GAGFYKGMVS ALRMKTFNMD SLIAIGTSVA
     FFYSVVNFMT YYAVNNSIIG LAGAKIPDLY FETAAFLITF VLLGKFLEAK AKGRTSEAIK
     KLMGLQAKTA RVIRNWQTLD IPVDQVVKDD IIVVRPGEKV PVDGVITKGS SAIDESMITG
     ESLPVEKHID DNVIGGTINK LGSFEFCATR IGSETTLSQI IRLVEDAQGS KAPIQAVADK
     ISAWFVPAVI AVATLTFIVW FFVLGSSLAF ALMAFTAVIV IACPCALGLA TPTAIMVGTG
     VGAEHGILVK GGEPLESASK INTIVFDKTG TITKGKPEVT DIEDLSDLDE EEVLTIAASL
     EKQSEHPLAE AIVNYAEVEK FALSGVVGFE AIPGHGVKGK IGKTDYYLGN RKLMIDKLNL
     DIDKFERKLE RLEDAGKTAM ILADKKGILG IVAVADTVKE TSKEAVEMLK GSGIEVWMIT
     GDNLRTANAI AMQVGITNIL AEVLPGEKAE RIKELQGGLP AGRRVAMVGD GINDAPALAQ
     ADLGIAMGSG TDVAMETGGI VIIKNDLRDV VNALDLSKTT VSKIRQNMFF ALFYNVIGIP
     VAARVFAFMG LILKPELAGL AMALSSVSVV GNSLLLRKYQ PGKKNYLSMY APYAMMLAFT
     FLFFEFARFS SSGMGK
//
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