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
//