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Database: UniProt
Entry: A0A103E814_9BURK
LinkDB: A0A103E814_9BURK
Original site: A0A103E814_9BURK 
ID   A0A103E814_9BURK        Unreviewed;       869 AA.
AC   A0A103E814;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Copper-transporting ATPase {ECO:0000313|EMBL:KVE30095.1};
GN   ORFNames=WS67_03935 {ECO:0000313|EMBL:KVE30095.1};
OS   Burkholderia singularis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=1503053 {ECO:0000313|EMBL:KVE30095.1, ECO:0000313|Proteomes:UP000062788};
RN   [1] {ECO:0000313|EMBL:KVE30095.1, ECO:0000313|Proteomes:UP000062788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSV85 {ECO:0000313|EMBL:KVE30095.1,
RC   ECO:0000313|Proteomes:UP000062788};
RA   Sahl J., Keim P., Wagner D.;
RT   "Expanding the genomic diversity of Burkholderia species for the
RT   development of highly accurate diagnostics.";
RL   Submitted (NOV-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:KVE30095.1}.
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DR   EMBL; LOWA01000008; KVE30095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A103E814; -.
DR   Proteomes; UP000062788; 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:UP000062788};
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..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        252..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        283..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        311..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        467..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        500..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        820..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        845..862
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          23..88
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          112..177
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          185..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  88783 MW;  C23746665AC7A68F CRC64;
     MDDQSATTTA SVAATAPPAP SPAVIELDIG GMTCASCAGR VEKALSRVPG VVSASVNLAT
     EKATVDAAPG VGTATLVDAV RRAGYRASAI DDQSATTTAS VAATAPPAPS PAVIELDIGG
     MTCASCAGRV EKALSRVPGV VSASVNLATE KATVDAAPGV GTATLVDAVR RAGYRASAID
     GIAPPTAETA ETSASAASPP PSAPATHSGA GERKLAEARR ERGLMIASAV LSAPLVWPML
     VAPFGIDATL PASLQLVLAS IVQFGFGARF YRAAWHALIA RAGNMDLLVA LGTSAAYGLS
     LWLMLRGEPG HPAHLYFEAS AVIITLVRLG KWLEARAKRQ TTDAIRALDA LRPERARVVE
     HGVERDVPLA QVRVGTSVRV RPGERIPVDG RIAAGVTHVD ESLITGESLP VPKQPGERVT
     AGSINGEGAL TVETTAIGAE TALARIIRLV ESAQAGKAPI QRLVDRVSAV FVPAIIAIAL
     VTLAGWLAAG ASAETAILNA VAVLVIACPC ALGLATPAAI MAGTGAAARR GMLIKDALAL
     ELAQRTRIVA FDKTGTLTEG RPTVTALEAI EIPHADALAL AATVQRDSTH PLARAVAAAF
     AADIAAHRSP FADAPAHAPR AVAGRGVEAN IDGQLIAFGS TRWRDELGIG VPAGIAQRAA
     ALEAAGHTVS WLMRIDVPRA ALALVAFGDT VKPQARTAIE RLAARGIRSA LVTGDNRGSA
     EAVAASLGID DVHAQVLPDD KARVVAQMKQ KAGGGMVAMV GDGINDAPAL AAADVGIAMA
     TGTDVAMHTA SITLMRGDPA LVADAIDISR RTYRKIQQNL FWAFAYNLIG IPLAALGWLN
     PMIAGAAMAF SSVSVVANAL LLRRWKGKA
//
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