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Database: UniProt
Entry: A0A0N1B1R8_9PROT
LinkDB: A0A0N1B1R8_9PROT
Original site: A0A0N1B1R8_9PROT 
ID   A0A0N1B1R8_9PROT        Unreviewed;       803 AA.
AC   A0A0N1B1R8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Copper-transporting ATPase {ECO:0000313|EMBL:KPF66643.1};
GN   ORFNames=IP84_15505 {ECO:0000313|EMBL:KPF66643.1};
OS   beta proteobacterium AAP99.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523428 {ECO:0000313|EMBL:KPF66643.1, ECO:0000313|Proteomes:UP000037960};
RN   [1] {ECO:0000313|EMBL:KPF66643.1, ECO:0000313|Proteomes:UP000037960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP99 {ECO:0000313|EMBL:KPF66643.1,
RC   ECO:0000313|Proteomes:UP000037960};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF66643.1}.
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DR   EMBL; LJIA01000020; KPF66643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1B1R8; -.
DR   STRING; 1523428.IP84_15505; -.
DR   PATRIC; fig|1523428.3.peg.1980; -.
DR   OrthoDB; 8552908at2; -.
DR   Proteomes; UP000037960; 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   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
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; 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; 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; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 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   Reference proteome {ECO:0000313|Proteomes:UP000037960};
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        164..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        191..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        224..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        252..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        404..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        437..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        754..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        779..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          2..73
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          75..140
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   803 AA;  82763 MW;  30E7DEC7855CEC45 CRC64;
     MQTLTLPISG MTCASCVARV ERALATVPGV LQATVNLATE SARLDVEPPK SSPLADAATA
     AVQAIERTGF AVPRLGVDLQ ISGMTCAACA GRVERALVQA PGVLSATVNL ADERAHVQLL
     AGTATAALTQ ALERAGYHGT PLQDDAQRAQ AEALAQAQAR KDRIAVWGSA LLTLPLALPM
     IGLLWGQHWM LPGWLQLLLA TPVQFVFGAR FYRAGWHAAR AGSGNMDLLV ALGTSAAFGL
     SLFNLWADPH HLYFESAAVV ITLVLLGKWL EARAKRKTTA AIRALQALAP DTATVMIDGQ
     PRSLPTAQLK VGDLLLVAPG EAVAADAVIV EGTSQLNESM LTGESLPVAR ALGDAIVGGS
     VNGEGRLVAR ISAVGRESLL ARIVHQVEQA QTRKAPVQRL VDQVAAVFVP VVLAIALGTL
     LGWGLSTGQW STALINAVAV LVIACPCALG LATPAALMAG TGVAARHGIL IKDAEALERA
     HRLKVVAFDK TGTLTIGQPR VVDVAAAEGA SDAELLSKAA ALSAGSAHPL AHALIAHASA
     LGDAMPLIAH DIQALAGYGL QGRIGTQIYA LGSGRYMAQL GVATTALSRA EATALAQGHS
     VSWLAELPAP GGSERPHLIG MIGFGDTPRP QSAAAVAALK RLNIRPVLLS GDHASAARHI
     GELLGIEDIH AQVLPSDKAA HVEKLKHFGP VAMVGDGIND APALAAADVG VAMGSGSDVA
     MNTAAITLMA NDPARVADAI DISRATVRKI RQNLFWAFGY NAIGIPLAAL GLLSPVLAGA
     AMALSSISVI SNALLLNRWS PKR
//
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