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Database: UniProt
Entry: A0A0E4CUC5_9BACL
LinkDB: A0A0E4CUC5_9BACL
Original site: A0A0E4CUC5_9BACL 
ID   A0A0E4CUC5_9BACL        Unreviewed;       817 AA.
AC   A0A0E4CUC5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE            EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE   AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE   AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN   Name=copA {ECO:0000313|EMBL:CQR51838.1};
GN   ORFNames=PRIO_0511 {ECO:0000313|EMBL:CQR51838.1};
OS   Paenibacillus riograndensis SBR5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC   Paenibacillus sonchi group.
OX   NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR51838.1, ECO:0000313|Proteomes:UP000033163};
RN   [1] {ECO:0000313|Proteomes:UP000033163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:456216; EC=7.2.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001390};
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; LN831776; CQR51838.1; -; Genomic_DNA.
DR   RefSeq; WP_020427221.1; NZ_LN831776.1.
DR   AlphaFoldDB; A0A0E4CUC5; -.
DR   STRING; 483937.AMQ84_27350; -.
DR   KEGG; pri:PRIO_0511; -.
DR   PATRIC; fig|1073571.4.peg.517; -.
DR   HOGENOM; CLU_001771_0_3_9; -.
DR   Proteomes; UP000033163; Chromosome I.
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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   NCBIfam; TIGR00003; copper ion binding protein; 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; 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   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:ARBA00023065};
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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:ARBA00022448}.
FT   TRANSMEM        167..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        231..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        267..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        418..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        453..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        769..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          10..76
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          78..144
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   817 AA;  86257 MW;  5333676B04C17D41 CRC64;
     MEKTAETPLQ QTTLQITGMT CSACAARIEK GLSRMEGVSK ANVNLALEQA TVGYDPAVAG
     VPQIEEKIRS LGYDTRKESA DFDISGMTCA ACSARIEKVL GRTPGIAAVN VNLALETAHV
     EYAPGSIGVS EIMEKVSSIG YKATLKQDRK EQADQRGQEI RHKRNKWIIS AILSFPLLWA
     MAGHFSFTEW IWTPELLMNP WFQLALATPV QFIIGWKFYV GAYKAVRNGS ANMDVLVVLG
     TSAAYFYSLY LTIDSLSMSG MSHTVDMYYE TSAVLITLIL VGKWSEALAK GRSSDAIRSL
     MGLQAKTALV VRDGAELSIP VEEVIPGDIV LVKPGTKVPV DGEVVEGLSS VDESMLTGES
     IPVEKKPGDS VIGGTLNKNG MLRIKARKVG RDTALAQIIR VVEEAQGSKA PIQRIADVIS
     GIFVPIVVGI AAVTFVIWFL WGAPGQFAEA LENAIAVLVI ACPCALGLAT PTSIMAGSGR
     AAEFGILFKG GEHLEAAQGI QVVVLDKTGT VTSGKPVLTD ILTTTGIAAH GKETAENRLL
     ALTAAAEKLS EHPLADAIVA GAAARGLELP EAGEFRAVPG RGITAVVGGQ TVSVGTRRMM
     EEGGAEPGPW APLMTKLEQE GKTAMLVSVE GVIAGVVAVA DTIKETSRAA VAKLHDMGIE
     VVMITGDNRI TAQAIAEQAG IRTVLAEVLP EGKAAEIRRL QSGGVKVAMV GDGINDAPAL
     ATADTGMAIG TGTDVAMEAA DITLMRGDLM SIPDAVMMSR RTMRNIKQNL FWALAYNTIG
     IPIAALGFLA PWLAGAAMAF SSVSVVLNAL RLQRVKL
//
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