COPA_SALTY
ID COPA_SALTY Reviewed; 833 AA.
AC Q8ZR95;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
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=STM0498;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION IN COPPER TOLERANCE, REGULATION BY CUER, INDUCTION BY COPPER, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=17768242; DOI=10.1099/mic.0.2007/006536-0;
RA Espariz M., Checa S.K., Perez Audero M.E., Pontel L.B., Soncini F.C.;
RT "Dissecting the Salmonella response to copper.";
RL Microbiology 153:2989-2997(2007).
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). Essential for copper tolerance under both aerobic and
CC anaerobic conditions (PubMed:17768242). {ECO:0000250|UniProtKB:Q59385,
CC ECO:0000269|PubMed:17768242}.
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=Q8ZR95-1; Sequence=Displayed;
CC Name=Soluble copper chaperone CopA(Z);
CC IsoId=Q8ZR95-2; Sequence=VSP_059179;
CC -!- INDUCTION: Transcriptionally up-regulated by CueR in response to copper
CC ions. {ECO:0000269|PubMed:17768242}.
CC -!- DISRUPTION PHENOTYPE: Causes a mild defect in aerobic growth on
CC CuSO(4), strongly impairs survival during anaerobic growth on CuSO(4).
CC {ECO:0000269|PubMed:17768242}.
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; AE006468; AAL19452.1; -; Genomic_DNA.
DR RefSeq; NP_459493.1; NC_003197.2. [Q8ZR95-1]
DR RefSeq; WP_000083899.1; NC_003197.2.
DR AlphaFoldDB; Q8ZR95; -.
DR SMR; Q8ZR95; -.
DR STRING; 99287.STM0498; -.
DR PaxDb; Q8ZR95; -.
DR EnsemblBacteria; AAL19452; AAL19452; STM0498.
DR GeneID; 1252018; -.
DR KEGG; stm:STM0498; -.
DR PATRIC; fig|99287.12.peg.532; -.
DR HOGENOM; CLU_001771_0_3_6; -.
DR OMA; ITFFGWM; -.
DR PhylomeDB; Q8ZR95; -.
DR BioCyc; SENT99287:STM0498-MON; -.
DR Proteomes; UP000001014; 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:0016020; C:membrane; IBA:GO_Central.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
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; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 1: Evidence at protein level;
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..833
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000046323"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 778..798
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 800..820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3..64
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 98..161
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 522
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 109
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 112
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 719
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 723
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT VAR_SEQ 70..833
FT /note="AKPLTESSIPSEALAAVPHELPVATADEESQQLLLSGMSCASCVTRVQHALQ
FT SVPGVTQARVNLAERTALVMGSASAADLVQAVEKAGYGAEAIEDDIKRRERQQETAIAT
FT MKRFRWQAIVALAVGIPVMVWGMIGDNMMVTDDNRSLWLAIGLITLAVMVFAGGHFYRN
FT AWKSLLNGTATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLG
FT HMLEARARQRSSKALEKLLDLTPPTARVVTEDGEKSVPLADVQPGMLLRLTTGDRVPVD
FT GEITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIR
FT MVRQAQSSKPEIGQLADKISAVFVPVVVAIALFSAAIWYFFGPAPQIVYTLVIATTVLI
FT IACPCALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTLVFDKTGTLTEGKPQV
FT VAIKTFNGVEEAQALRLAAALEQGSSHPLAHAILEKAGDDKLPQVNGFRTLRGLGVSGE
FT AEGHQLLLGNQALLNEQHVATDDMTAEITAQASQGSTPVLLAIDGKAAALLAVRDPLRS
FT DSIAALERLHNAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKADAIKRLQSQG
FT RQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATL
FT RNMKQNLLGAFIYNSIGIPVAAGILWPFTGTLLNPVVAGAAMALSSITVVSNANRLLRF
FT KPKA -> G (in isoform Soluble copper chaperone CopA(Z))"
FT /evidence="ECO:0000305|PubMed:28107647"
FT /id="VSP_059179"
SQ SEQUENCE 833 AA; 87910 MW; 5A56C403D54BCA09 CRC64;
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VELADVTVTE AHVTGTASAD ALIETIKQAG
YGATLSHPKA KPLTESSIPS EALAAVPHEL PVATADEESQ QLLLSGMSCA SCVTRVQHAL
QSVPGVTQAR VNLAERTALV MGSASAADLV QAVEKAGYGA EAIEDDIKRR ERQQETAIAT
MKRFRWQAIV ALAVGIPVMV WGMIGDNMMV TDDNRSLWLA IGLITLAVMV FAGGHFYRNA
WKSLLNGTAT MDTLVALGTG VAWLYSMSVN LWPQWFPMEA RHLYYEASAM IIGLINLGHM
LEARARQRSS KALEKLLDLT PPTARVVTED GEKSVPLADV QPGMLLRLTT GDRVPVDGEI
TQGEAWLDEA MLTGEPIPQQ KGEGDSVHAG TVVQDGSVLF RASAVGSHTT LSRIIRMVRQ
AQSSKPEIGQ LADKISAVFV PVVVAIALFS AAIWYFFGPA PQIVYTLVIA TTVLIIACPC
ALGLATPMSI ISGVGRAAEF GVLVRDADAL QRASTLDTLV FDKTGTLTEG KPQVVAIKTF
NGVEEAQALR LAAALEQGSS HPLAHAILEK AGDDKLPQVN GFRTLRGLGV SGEAEGHQLL
LGNQALLNEQ HVATDDMTAE ITAQASQGST PVLLAIDGKA AALLAVRDPL RSDSIAALER
LHNAGYRLVM LTGDNPTTAN AIAKEAGIDE VIAGVLPDGK ADAIKRLQSQ GRQVAMVGDG
INDAPALAQA DVGIAMGGGS DVAIETAAIT LMRHSLMGVA DALAISRATL RNMKQNLLGA
FIYNSIGIPV AAGILWPFTG TLLNPVVAGA AMALSSITVV SNANRLLRFK PKA
