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Database: UniProt
Entry: A0A1Q8IMQ7_9BURK
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ID   A0A1Q8IMQ7_9BURK        Unreviewed;       917 AA.
AC   A0A1Q8IMQ7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Copper-transporting ATPase {ECO:0000313|EMBL:OLL27966.1};
GN   ORFNames=BTH42_30250 {ECO:0000313|EMBL:OLL27966.1};
OS   Burkholderia sp. SRS-W-2-2016.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1926878 {ECO:0000313|EMBL:OLL27966.1, ECO:0000313|Proteomes:UP000186182};
RN   [1] {ECO:0000313|Proteomes:UP000186182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRS-W-2-2016 {ECO:0000313|Proteomes:UP000186182};
RA   Chauhan A.;
RL   Submitted (DEC-2016) 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:OLL27966.1}.
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DR   EMBL; MSDV01000073; OLL27966.1; -; Genomic_DNA.
DR   RefSeq; WP_075304855.1; NZ_MSDV01000073.1.
DR   AlphaFoldDB; A0A1Q8IMQ7; -.
DR   STRING; 1926878.BTH42_30250; -.
DR   OrthoDB; 8552908at2; -.
DR   Proteomes; UP000186182; 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:0005507; F:copper ion binding; IEA:InterPro.
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; IPR006122; HMA_Cu_ion-bd.
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   NCBIfam; TIGR00003; copper ion binding protein; 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; 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; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 2.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
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   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022796};
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:UP000186182};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT   TRANSMEM        238..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        268..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        299..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        327..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        485..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        512..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        860..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        885..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          26..91
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          114..194
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   917 AA;  93844 MW;  EB54145311F58BBB CRC64;
     MTGLADPQRP ADAASSSPSP SPTPARVVEI DVGGMTCASC AMRVEKALAK VPGVARASVN
     LATERARVES TATVAAEQLA DAVRNAGYDA TLVASADAVA PAEASLAASA DAAAATELQI
     GGMTCASCAM RVEKALAKVP GVARASVNLA TETATVYAEH AAAGNAAAAN ANADVDVDVD
     ALIAAVKKAG YEATLSAPPA SPAAFGASAS AATATDESDT PPQPSLAERK QSEARRDLAS
     VVASALLTLP LVAPMFGEWF GIHAMPPAWL QLVLASIVQF VFGARFYRAA WRALRAGAGN
     MDLLVALGTS AAYGISVYEL ASHPGDMMHL YFEASAVVIT LVRFGKWLEA RAKRQTTDAI
     RALNALRPER ARIRVGGEER DVPLAQVRVG TVVVVRPGER VPVDGAVLEG RSHIDEALIT
     GESLPVPKQT GDAVTAGSIN GEGVLAVTTT AIGAETTLAR IIRLVESAQA EKAPIQRLVD
     RVSELFVPAI LAIAALTLVG WLLAGAGGET AILNAVAVLV IACPCALGLA TPAAIMAGTG
     VAARHGVLIK DAEALEIAHR VSIVAFDKTG TLTLGQPSVT AFEPVGALGR KAALALAAAV
     QRHSEHPLAR AVVSAYEAEP GAKEPAHEGL AAATERVPVD HATAAASDQA AAAPHASAAR
     AVAGRGVEAE VDGRTLALGS TRWLRELGID LPPALAVRAQ ELEAAGNTVS WLMTRAPHAP
     EALALIAFGD TVKPSARAAV ERLKRMGIRS VLVTGDNRGS AASVAQALGI DEFHAEVLPD
     DKARVIRDLK IRHAGIVAMA GDGINDAPAL AAADIGIAMA TGTDVAMHAA GVTLMRGDPA
     LVADAIDISR RTWRKIQQNL FWAFVYNLIG IPLAAFGLLN PMLAGAAMAF SSVSVVTNAL
     LLRTWRGGPG GAAGPAR
//
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