COPA_ECO57
ID COPA_ECO57 Reviewed; 834 AA.
AC Q8XD24;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Copper-exporting P-type ATPase;
DE EC=7.2.2.8;
DE AltName: Full=Copper-exporting P-type ATPase A;
DE AltName: Full=Cu(+)-exporting ATPase;
DE AltName: Full=Soluble copper chaperone CopA(Z) {ECO:0000250|UniProtKB:Q59385};
GN Name=copA; OrderedLocusNames=Z0604, ECs0537;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP POSSIBLE RIBOSOMAL FRAMESHIFT TO TRANSLATE ISOFORM SOLUBLE COPPER CHAPERONE
RP COPA(Z).
RX PubMed=28107647; DOI=10.1016/j.molcel.2016.12.008;
RA Meydan S., Klepacki D., Karthikeyan S., Margus T., Thomas P., Jones J.E.,
RA Khan Y., Briggs J., Dinman J.D., Vazquez-Laslop N., Mankin A.S.;
RT "Programmed ribosomal frameshifting generates a copper transporter and a
RT copper chaperone from the same gene.";
RL Mol. Cell 65:207-219(2017).
CC -!- FUNCTION: [Copper-exporting P-type ATPase]: Involved in Cu(+) export
CC (By similarity). {ECO:0000250|UniProtKB:Q59385}.
CC -!- FUNCTION: [Isoform Soluble copper chaperone CopA(Z)]: Probably also
CC encodes a cytoplasmic copper chaperone CopA(Z) that is produced by
CC programmed ribosomal frameshifting (Probable).
CC {ECO:0000250|UniProtKB:Q59385, ECO:0000305|PubMed:28107647}.
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 -!- SUBCELLULAR LOCATION: [Copper-exporting P-type ATPase]: Cell inner
CC membrane {ECO:0000250|UniProtKB:Q59385}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q59385}.
CC -!- SUBCELLULAR LOCATION: [Isoform Soluble copper chaperone CopA(Z)]:
CC Cytoplasm {ECO:0000250|UniProtKB:Q59385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Copper-exporting P-type ATPase A;
CC IsoId=Q8XD24-1; Sequence=Displayed;
CC Name=Soluble copper chaperone CopA(Z);
CC IsoId=Q8XD24-2; Sequence=VSP_059177;
CC -!- MISCELLANEOUS: [Isoform Soluble copper chaperone CopA(Z)]: Expression
CC of the CopA(Z) soluble copper chaperone isoform requires a -1
CC programmed ribosomal frameshift (PRF) at the 70th codon. A nucleotide
CC 'slippery sequence' that promotes PRF is found just downstream of the
CC frameshifted site. {ECO:0000250|UniProtKB:Q59385,
CC ECO:0000305|PubMed:28107647}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG54833.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33960.1; -; Genomic_DNA.
DR PIR; A90696; A90696.
DR PIR; E85546; E85546.
DR RefSeq; NP_308564.1; NC_002695.1.
DR RefSeq; WP_000083954.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XD24; -.
DR SMR; Q8XD24; -.
DR STRING; 155864.EDL933_0561; -.
DR EnsemblBacteria; AAG54833; AAG54833; Z0604.
DR EnsemblBacteria; BAB33960; BAB33960; ECs_0537.
DR GeneID; 914641; -.
DR KEGG; ece:Z0604; -.
DR KEGG; ecs:ECs_0537; -.
DR PATRIC; fig|386585.9.peg.644; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_6; -.
DR OMA; ITFFGWM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.
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; 2.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 2.
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; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Copper; Copper transport;
KW Cytoplasm; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ribosomal frameshifting; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..834
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000046321"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3..64
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 99..162
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 523
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 14
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 17
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 110
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 113
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 724
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT VAR_SEQ 70..834
FT /note="AKPLAESSIPSEALTAVSEALPAATADDDDSQQLLLSGMSCASCVTRVQNAL
FT QSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYGAEAIEDDAKRRERQQETAVA
FT TMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYR
FT SAWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINL
FT GHMLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPV
FT DGEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRII
FT RMVRQAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVL
FT IIACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQ
FT VVAVKTFADFDEAQALRLAAALEQGSSHPLARAILDKASDMQLPQVNGFRTLRGLGVSG
FT EAEGHALLLGNQALLNDQQVDTKAIEADISAQASQGATPVLLAVDGKAVALLAVRDPLR
FT SDSVAALQRLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKRLQSE
FT GRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRAT
FT LRNMKQNLLGAFIYNSIGIPVAAGILWPFTGTLLNPVVAGAAMALSSITVVSNANRLLR
FT FKPKE -> G (in isoform Soluble copper chaperone CopA(Z))"
FT /evidence="ECO:0000305|PubMed:28107647"
FT /id="VSP_059177"
SQ SEQUENCE 834 AA; 88005 MW; B4789F2CCF12E9FB CRC64;
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG
YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA
LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA
TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS
AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE
ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR
QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP
CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT
FADFDEAQAL RLAAALEQGS SHPLARAILD KASDMQLPQV NGFRTLRGLG VSGEAEGHAL
LLGNQALLND QQVDTKAIEA DISAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ
RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKRLQS EGRQVAMVGD
GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LRNMKQNLLG
AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE
