COPA_LEGPH
ID COPA_LEGPH Reviewed; 736 AA.
AC Q5ZWR1;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000305};
DE EC=7.2.2.8 {ECO:0000269|PubMed:24317491};
DE AltName: Full=Copper-exporting P-type ATPase A;
DE AltName: Full=Copper-transporting PIB-type ATPase {ECO:0000303|PubMed:21716286};
DE AltName: Full=Cu(+)-ATPase LpCopA {ECO:0000303|PubMed:21716286};
GN Name=copA {ECO:0000303|PubMed:21716286};
GN OrderedLocusNames=lpg1024 {ECO:0000312|EMBL:AAU27110.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [2] {ECO:0007744|PDB:3RFU}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), AND FUNCTION AS AN ATPASE.
RX PubMed=21716286; DOI=10.1038/nature10191;
RA Gourdon P., Liu X.Y., Skjorringe T., Morth J.P., Moller L.B.,
RA Pedersen B.P., Nissen P.;
RT "Crystal structure of a copper-transporting PIB-type ATPase.";
RL Nature 475:59-64(2011).
RN [3] {ECO:0007744|PDB:4BEV}
RP X-RAY CRYSTALLOGRAPHY (3.58 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP PHOSPHATE ANALOG, AND ACTIVE SITE.
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RA Mattle D., Drachmann N.D., Liu X.Y., Gourdon P., Pedersen B.P., Morth P.,
RA Wang J., Nissen P.;
RT "ATPase crystal structure with bound phosphate analogue.";
RL Submitted (MAR-2013) to the PDB data bank.
RN [4] {ECO:0007744|PDB:4BYG}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP PHOSPHATE ANALOG, AND ACTIVE SITE.
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RA Mattle D., Drachmann N.D., Liu X.Y., Pedersen B.P., Morth J.P., Wang J.,
RA Gourdon P., Nissen P.;
RT "Dephosphorylation of PIB-type Cu(I)-ATPases as studied by metallofluoride
RT complexes.";
RL Submitted (JUL-2013) to the PDB data bank.
RN [5] {ECO:0007744|PDB:4BBJ}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COPPER-BINDING SITES, AND
RP MUTAGENESIS OF PRO-94; MET-100; GLU-189; ASP-426; PRO-710; MET-711; ALA-714
RP AND MET-717.
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=24317491; DOI=10.1038/nsmb.2721;
RA Andersson M., Mattle D., Sitsel O., Klymchuk T., Nielsen A.M., Moller L.B.,
RA White S.H., Nissen P., Gourdon P.;
RT "Copper-transporting P-type ATPases use a unique ion-release pathway.";
RL Nat. Struct. Mol. Biol. 21:43-48(2014).
CC -!- FUNCTION: Couples the hydrolysis of ATP with the export of copper.
CC {ECO:0000269|PubMed:24317491, ECO:0000305|PubMed:21716286}.
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:24317491};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:24317491}; Multi-pass membrane protein
CC {ECO:0000255}.
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; AE017354; AAU27110.1; -; Genomic_DNA.
DR RefSeq; WP_010946759.1; NC_002942.5.
DR RefSeq; YP_095057.1; NC_002942.5.
DR PDB; 3RFU; X-ray; 3.20 A; A/B/C/D=1-736.
DR PDB; 4BBJ; X-ray; 2.75 A; A=1-736.
DR PDB; 4BEV; X-ray; 3.58 A; A=1-736.
DR PDB; 4BYG; X-ray; 2.85 A; A=1-736.
DR PDBsum; 3RFU; -.
DR PDBsum; 4BBJ; -.
DR PDBsum; 4BEV; -.
DR PDBsum; 4BYG; -.
DR AlphaFoldDB; Q5ZWR1; -.
DR SMR; Q5ZWR1; -.
DR STRING; 272624.lpg1024; -.
DR PaxDb; Q5ZWR1; -.
DR EnsemblBacteria; AAU27110; AAU27110; lpg1024.
DR GeneID; 66490203; -.
DR KEGG; lpn:lpg1024; -.
DR PATRIC; fig|272624.6.peg.1064; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_6; -.
DR OMA; ACGMNMV; -.
DR BRENDA; 7.2.2.8; 14579.
DR Proteomes; UP000000609; 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 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; IPR045800; HMBD.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF19335; HMBD; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Copper;
KW Copper transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..736
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000439348"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305|Ref.3, ECO:0000305|Ref.4"
FT BINDING 426
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24317491, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4BBJ,
FT ECO:0007744|PDB:4BEV, ECO:0007744|PDB:4BYG"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24317491, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4BBJ,
FT ECO:0007744|PDB:4BEV, ECO:0007744|PDB:4BYG"
FT BINDING 624
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24317491, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:4BBJ,
FT ECO:0007744|PDB:4BEV, ECO:0007744|PDB:4BYG"
FT SITE 189
FT /note="Important for copper transport"
FT /evidence="ECO:0000303|PubMed:24317491"
FT SITE 382
FT /note="Important for copper transport"
FT /evidence="ECO:0000303|PubMed:24317491"
FT SITE 384
FT /note="Important for copper transport"
FT /evidence="ECO:0000303|PubMed:24317491"
FT SITE 717
FT /note="Important for copper transport"
FT /evidence="ECO:0000303|PubMed:24317491"
FT MUTAGEN 94
FT /note="P->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 100
FT /note="M->E: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 100
FT /note="M->L: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 189
FT /note="E->N: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 189
FT /note="E->Q: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 426
FT /note="D->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 710
FT /note="P->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 711
FT /note="M->L: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 714
FT /note="A->T: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT MUTAGEN 717
FT /note="M->V: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24317491"
FT HELIX 76..101
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:4BBJ"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 148..168
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4BYG"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3RFU"
FT HELIX 188..217
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:4BYG"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4BBJ"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:4BYG"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3RFU"
FT STRAND 260..272
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:3RFU"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 314..327
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 335..361
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 366..381
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 386..402
FT /evidence="ECO:0007829|PDB:4BBJ"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:4BBJ"
FT TURN 427..430
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 437..446
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 448..459
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:4BBJ"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 509..515
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 520..531
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 544..552
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 559..568
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 572..579
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 581..590
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 602..614
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 629..634
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 635..641
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 646..651
FT /evidence="ECO:0007829|PDB:4BBJ"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:4BYG"
FT HELIX 662..697
FT /evidence="ECO:0007829|PDB:4BBJ"
FT TURN 698..703
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 710..728
FT /evidence="ECO:0007829|PDB:4BBJ"
FT HELIX 729..733
FT /evidence="ECO:0007829|PDB:4BBJ"
SQ SEQUENCE 736 AA; 78244 MW; E95CC6FAF47AAC45 CRC64;
MKHDHHQGHT HSGKGHACHH EHNSPKTQQA SSKMEGPIVY TCPMHPEIRQ SAPGHCPLCG
MALEPETVTV SEVVSPEYLD MRRRFWIALM LTIPVVILEM GGHGLKHFIS GNGSSWIQLL
LATPVVLWGG WPFFKRGWQS LKTGQLNMFT LIAMGIGVAW IYSMVAVLWP GVFPHAFRSQ
EGVVAVYFEA AAVITTLVLL GQVLELKARE QTGSAIRALL KLVPESAHRI KEDGSEEEVS
LDNVAVGDLL RVRPGEKIPV DGEVQEGRSF VDESMVTGEP IPVAKEASAK VIGATINQTG
SFVMKALHVG SDTMLARIVQ MVSDAQRSRA PIQRLADTVS GWFVPAVILV AVLSFIVWAL
LGPQPALSYG LIAAVSVLII ACPCALGLAT PMSIMVGVGK GAQSGVLIKN AEALERMEKV
NTLVVDKTGT LTEGHPKLTR IVTDDFVEDN ALALAAALEH QSEHPLANAI VHAAKEKGLS
LGSVEAFEAP TGKGVVGQVD GHHVAIGNAR LMQEHGGDNA PLFEKADELR GKGASVMFMA
VDGKTVALLV VEDPIKSSTP ETILELQQSG IEIVMLTGDS KRTAEAVAGT LGIKKVVAEI
MPEDKSRIVS ELKDKGLIVA MAGDGVNDAP ALAKADIGIA MGTGTDVAIE SAGVTLLHGD
LRGIAKARRL SESTMSNIRQ NLFFAFIYNV LGVPLAAGVL YPLTGLLLSP MIAAAAMALS
SVSVIINALR LKRVTL
