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Database: UniProt
Entry: A0A1B3PLN4_9BURK
LinkDB: A0A1B3PLN4_9BURK
Original site: A0A1B3PLN4_9BURK 
ID   A0A1B3PLN4_9BURK        Unreviewed;       774 AA.
AC   A0A1B3PLN4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:AOG23699.1};
DE            EC=3.6.3.4 {ECO:0000313|EMBL:AOG23699.1};
GN   ORFNames=BSY15_1506 {ECO:0000313|EMBL:AOG23699.1};
OS   Acidovorax sp. RAC01.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1842533 {ECO:0000313|EMBL:AOG23699.1, ECO:0000313|Proteomes:UP000094760};
RN   [1] {ECO:0000313|Proteomes:UP000094760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC01 {ECO:0000313|Proteomes:UP000094760};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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}.
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DR   EMBL; CP016447; AOG23699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B3PLN4; -.
DR   STRING; 1842533.BSY15_1506; -.
DR   KEGG; acra:BSY15_1506; -.
DR   PATRIC; fig|1842533.3.peg.1570; -.
DR   Proteomes; UP000094760; Chromosome.
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; 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; 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; 1.
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; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 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   Hydrolase {ECO:0000313|EMBL:AOG23699.1};
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:UP000094760};
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        119..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        152..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        215..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        367..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        397..420
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        727..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        752..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          34..105
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   774 AA;  79712 MW;  C480C158CABFF96C CRC64;
     MLDLAIASRI TITAMNTSAT PSTPSSLPGN APAQALDIGI GGMTCASCVG RVERALRKVP
     GVQEASVNLA TESARIAFVA STAADTAAMD ALLRRAVRNA GYEPRAADAA DAADDASPWA
     GFMPVAIGLA LSAPLVLPML GDLFGQHWML PAWVQFALAT PVQFILGARF YKAGWHAAKA
     LSGNMDLLVA LGTSAGWGLS VWLWLTAHAG HTPHLYFEAS AVVITLVLLG KWLEARAKQQ
     TTAAIRALHA LRPDVVHLLG KDGEVDVPVA EVLAGDRLVV RPGERFPVDG VVREGHTQVD
     ESMLTGEPLP VPRDVGAPVT GGSINGDGRV VVEVTAVGSE TVLAHIIRLV EDAQAAKAPI
     QRLVDQVSAV FVPVVLGIAL ITLGGWLAMG VGLESALIHA VAVMVIACPC ALGLATPAAI
     MAGTGVAARH GILIKDAQAL ELAHKVDTVA FDKTGTLTVG QPRLSAFEVV PGLDAAGVMA
     AVASVQSGSE HPLARAVAAA AAQQKLVVQP PDAVRAVPGR GTEGEVQGHG WLVGSLRWMD
     ELGVQALKDG PLADRAAALQ REGATVSAVA ERTDQGLALR AIMAFGDEPK PGAREALAAL
     KARGIRTVMI SGDNRGAAEV MARRLGLDPD AGEVMAEVLP GDKAAAVRAL QLGNAAGHPA
     HHTVAMVGDG VNDAPALAAA HVGMAMGNGT DVAMHAAGIT LMRGDPMLVA AALDISRRTV
     MKIRQNLFWA FAYNVAGIPL AALGYLSPVV AGAAMALSSV SVMANALLLK RWRL
//
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