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Database: UniProt
Entry: A0A1Q9S6R9_9PSEU
LinkDB: A0A1Q9S6R9_9PSEU
Original site: A0A1Q9S6R9_9PSEU 
ID   A0A1Q9S6R9_9PSEU        Unreviewed;       715 AA.
AC   A0A1Q9S6R9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Copper-transporting ATPase {ECO:0000313|EMBL:OLT05621.1};
GN   ORFNames=BJF90_00845 {ECO:0000313|EMBL:OLT05621.1};
OS   Pseudonocardia sp. CNS-004.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1904967 {ECO:0000313|EMBL:OLT05621.1, ECO:0000313|Proteomes:UP000186863};
RN   [1] {ECO:0000313|EMBL:OLT05621.1, ECO:0000313|Proteomes:UP000186863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-004 {ECO:0000313|EMBL:OLT05621.1,
RC   ECO:0000313|Proteomes:UP000186863};
RX   PubMed=27902408; DOI=10.1099/mic.0.000386;
RA   Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA   Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT   "Sequencing rare marine actinomycete genomes reveals high density of unique
RT   natural product biosynthetic gene clusters.";
RL   Microbiology 162:2075-2086(2016).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:OLT05621.1}.
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DR   EMBL; MKJV01000068; OLT05621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q9S6R9; -.
DR   Proteomes; UP000186863; 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   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; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_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; 1.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF19991; HMA_2; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 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};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186863};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   715 AA;  75709 MW;  5B4A7ABEF48362D3 CRC64;
     MIRVAVTVLS DAAGRVRFAA PGLVGSPALA VAVEDAVDTV VHVRQVHAYP RTGSIVVWYD
     PERCDRTELL EAVDKGLGAD PEATAERTPR SAEVRNGDLV RLAVGGAALA VLGIRRYGLR
     RPPVLGPSSR AVATGVTIFT GYPFLRGALR SMAGGRGAGT DALVSAATVA SLVLRENVVA
     LTVLWLLNIG EYLQDLTLRR SRRAISELLT GARTRTWMRL ADGTELEVDI DQLGVGDEVV
     VHEQVVLPVD GVVVEGDGVV DQAAITGEQL PVSVGVGTPL PAGSVLKRGR LVVRATAVGR
     DTAIGRIIAR VEEAQHDRAP IQTVGETFSR RFVPTSFALS ALTLLVTRDV RRAMTMLLVA
     CPCAVGLSTP TAISAAIGNG ARRGILIKGG AHLEAAGRVN AIVFDKTGTL TLGRPVVTNV
     VSFHDDWTPE QVLAYAASSE IHSRHPLAQA VIRSTEERRI EIPPHEECEV LLGQGMRVES
     DGRELLIGSR ELLRRQKVRV SRKAHDWVRR LQRATEIPLL LAVDGDLVGL VSLRDSIRPE
     SREVLDALRA DGVERIVLLT GDHPDVAAAV AAELGIDEFR AQVLPEQKQD VVRALQAEGY
     TVAVVGDGTN DAPALALSDI GIAMGVGGTD VAVETADVAL AGDDLRTLMD LRDLGRRGVG
     LIRQNYGMSI AVNAAGLLVS AAGGMSPVVA AILHNASSVA VVANSSRLIR YGLRP
//
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