COPA_ENTHA
ID COPA_ENTHA Reviewed; 727 AA.
AC P32113; I6TBM0; Q47841;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable copper-importing P-type ATPase A;
DE EC=7.2.2.8 {ECO:0000269|PubMed:11162579};
GN Name=copA; OrderedLocusNames=EHR_09085;
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN COPPER HOMEOSTASIS.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=8048974; DOI=10.1016/s0021-9258(18)31455-8;
RA Odermatt A., Suter H., Krapf R., Solioz M.;
RT "Primary structure of two P-type ATPases involved in copper homeostasis in
RT Enterococcus hirae.";
RL J. Biol. Chem. 268:12775-12779(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=22933757; DOI=10.1128/jb.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=7876197; DOI=10.1074/jbc.270.9.4349;
RA Odermatt A., Solioz M.;
RT "Two trans-acting metalloregulatory proteins controlling expression of the
RT copper-ATPases of Enterococcus hirae.";
RL J. Biol. Chem. 270:4349-4354(1995).
RN [4]
RP INDUCTION BY COPPER AND SILVER.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=8037745; DOI=10.1006/bbrc.1994.1891;
RA Odermatt A., Krapf R., Solioz M.;
RT "Induction of the putative copper ATPases, CopA and CopB, of Enterococcus
RT hirae by Ag+ and Cu2+, and Ag+ extrusion by CopB.";
RL Biochem. Biophys. Res. Commun. 202:44-48(1994).
RN [5]
RP INTERACTION WITH COPZ, AND MUTAGENESIS OF CYS-17 AND CYS-20.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=11594769; DOI=10.1006/bbrc.2001.5757;
RA Multhaup G., Strausak D., Bissig K.-D., Solioz M.;
RT "Interaction of the CopZ copper chaperone with the CopA copper ATPase of
RT Enterococcus hirae assessed by surface plasmon resonance.";
RL Biochem. Biophys. Res. Commun. 288:172-177(2001).
RN [6]
RP FUNCTION AS A COPPER ATPASE, CATALYTIC ACTIVITY, ACYLPHOSPHATE FORMATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459
RC / NCDO 1258 / NCTC 12367 / WDCM 00089 / R;
RX PubMed=11162579; DOI=10.1006/bbrc.2000.4176;
RA Wunderli-Ye H., Solioz M.;
RT "Purification and functional analysis of the copper ATPase CopA of
RT Enterococcus hirae.";
RL Biochem. Biophys. Res. Commun. 280:713-719(2001).
CC -!- FUNCTION: Probably involved in copper import under copper limiting
CC conditions. {ECO:0000269|PubMed:11162579, ECO:0000269|PubMed:8048974}.
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:0000269|PubMed:11162579};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate.
CC {ECO:0000269|PubMed:11162579}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for ATP {ECO:0000269|PubMed:11162579};
CC Vmax=0.15 umol/min/mg enzyme {ECO:0000269|PubMed:11162579};
CC pH dependence:
CC Optimum pH is 6.25. {ECO:0000269|PubMed:11162579};
CC -!- SUBUNIT: Monomer. Interacts with the copper chaperone CopZ.
CC {ECO:0000269|PubMed:11594769}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By copper and silver. {ECO:0000269|PubMed:8037745}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13292; AAA61835.1; -; Genomic_DNA.
DR EMBL; CP003504; AFM70729.1; -; Genomic_DNA.
DR EMBL; Z46807; CAA86837.1; -; Genomic_DNA.
DR PIR; A45995; A45995.
DR RefSeq; WP_010737925.1; NZ_KB946231.1.
DR AlphaFoldDB; P32113; -.
DR SMR; P32113; -.
DR STRING; 768486.EHR_09085; -.
DR TCDB; 3.A.3.5.1; the p-type atpase (p-atpase) superfamily.
DR EnsemblBacteria; AFM70729; AFM70729; EHR_09085.
DR KEGG; ehr:EHR_09085; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_9; -.
DR OrthoDB; 237367at2; -.
DR SABIO-RK; P32113; -.
DR Proteomes; UP000002895; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00403; HMA; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..727
FT /note="Probable copper-importing P-type ATPase A"
FT /id="PRO_0000046250"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..119
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..375
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 699..700
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 701..721
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 722..727
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 6..70
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 425
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 20
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 621
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 625
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 17
FT /note="C->S: Still strongly interacts with CopZ but
FT abolishes the modulating activity of copper; when
FT associated with S-20."
FT /evidence="ECO:0000269|PubMed:11594769"
FT MUTAGEN 20
FT /note="C->S: Still strongly interacts with CopZ but
FT abolishes the modulating activity of copper; when
FT associated with S-17."
FT /evidence="ECO:0000269|PubMed:11594769"
FT CONFLICT 630
FT /note="A -> R (in Ref. 1; AAA61835)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 78303 MW; 30A0858F2389B22B CRC64;
MATNTKMETF VITGMTCANC SARIEKELNE QPGVMSATVN LATEKASVKY TDTTTERLIK
SVENIGYGAI LYDEAHKQKI AEEKQTYLRK MKFDLIFSAI LTLPLMLAMI AMMLGSHGPI
VSFFHLSLVQ LLFALPVQFY VGWRFYKGAY HALKTKAPNM DVLVAIGTSA AFALSIYNGF
FPSHSHDLYF ESSSMIITLI LLGKYLEHTA KSKTGDAIKQ MMSLQTKTAQ VLRDGKEETI
AIDEVMIDDI LVIRPGEQVP TDGRIIAGTS ALDESMLTGE SVPVEKKEKD MVFGGTINTN
GLIQIQVSQI GKDTVLAQII QMVEDAQGSK APIQQIADKI SGIFVPIVLF LALVTLLVTG
WLTKDWQLAL LHSVSVLVIA CPCALGLATP TAIMVGTGVG AHNGILIKGG EALEGAAHLN
SIILDKTGTI TQGRPEVTDV IGPKEIISLF YSLEHASEHP LGKAIVAYGA KVGAKTQPIT
DFVAHPGAGI SGTINGVHYF AGTRKRLAEM NLSFDEFQEQ ALELEQAGKT VMFLANEEQV
LGMIAVADQI KEDAKQAIEQ LQQKGVDVFM VTGDNQRAAQ AIGKQVGIDS DHIFAEVLPE
EKANYVEKLQ KAGKKVGMVG DGINDAPALA LADVGIAMGS GTDIAMETAD VTLMNSHLTS
INQMISLSAA TLKKIKQNLF WAFIYNTIGI PFAAFGFLNP IIAGGAMAFS SISVLLNSLS
LNRKTIK
