ID A0A0G1BHC2_9BACT Unreviewed; 774 AA.
AC A0A0G1BHC2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE SubName: Full=Copper-transporting P-type ATPase {ECO:0000313|EMBL:KKS72737.1};
GN ORFNames=UV43_C0013G0005 {ECO:0000313|EMBL:KKS72737.1};
OS Parcubacteria group bacterium GW2011_GWF2_42_7.
OC Bacteria.
OX NCBI_TaxID=1618966 {ECO:0000313|EMBL:KKS72737.1, ECO:0000313|Proteomes:UP000033976};
RN [1] {ECO:0000313|EMBL:KKS72737.1, ECO:0000313|Proteomes:UP000033976}
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:KKS72737.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCEL01000013; KKS72737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1BHC2; -.
DR PATRIC; fig|1618966.3.peg.244; -.
DR Proteomes; UP000033976; 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; 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 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; 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; 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 94..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 119..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 370..393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 722..744
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 750..769
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 774 AA; 84177 MW; B8942C1F3E4142DE CRC64;
MKKEVFKIKG MHCASCARTI EKAVKKLNGI KKSEVNFASE TLLAEFDERE IGFNEIKKTV
AESGYQLLNK EKNEEVVLPH LHNHKEISLA KNKIIVGAIL SALIFLGSFP EWFKFVPAVF
NNYFLLFILT TPVQFWVGRS FYSGLKILFK YQRADMNTLI SVGTLAGYFY SSAVTFFPEF
FSRGGLQPKI YFDTSAIIIT LILLGRYLEL LAKGRASEAI KKLMKLSAKT ARVLKAGKET
EIPIEEVEAG DIVIVRPGEK IPVDGIVIEG KSEVDESMVT GESMPVFKGA GANVIGSTIN
QTGAFQFKAT KVGQETLLAQ IIKMVEQAQG SKAPIQRLAD IISGYFVPAV IGVAISTFII
WLIFGPAPAF TFALVNFVAV LIIACPCALG LATPMAMMVS IGKAAEKGIL IRDAASLEIA
NKIKTIVFDK TGTLTQGKPA VTDILNFNKE VASPREDATS GKATSEKEIL KIAASLEQKS
EHPIARAILE EAKKAVPPLA GRASSTQGGR ENLELFENKD FEAIPGKGIR GLLLIGGEKI
RAAIGNQEMM KQEGIQFASR RIENEIEKLE EEGKTVMLIL VSGKILGAIG VADVLKSEAK
ASVHKLKEMG LEVWLLTGDN ERTGRAIAQE VGIENVMAKV LPQDKVKKIQ ELQKQNKKVA
MVGDGINDAP ALAQSDLGIA MSEGTDIAME SANITLMRGD LTLIPEVLKI SDRTLKIVKQ
NLFWAFFYNS AFIPVAAGAL YPFFGILLNP IFAAIAMSAS SISVVLNSLR LKRG
//