ID   PLAS_SILLB              Reviewed;         165 AA.
AC   P07030;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Plastocyanin, chloroplastic;
DE   Flags: Precursor;
GN   Name=PETE;
OS   Silene latifolia subsp. alba (White campion) (Lychnis alba).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Sileneae; Silene;
OC   Silene subgen. Behenantha; Silene sect. Melandrium.
OX   NCBI_TaxID=52853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Smeekens S., de Groot M., van Binsbergen J., Weisbeek P.J.;
RT   "Sequence of the precursor of the chloroplast thylakoid lumen protein
RT   plastocyanin.";
RL   Nature 317:456-458(1985).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 67-165 IN COMPLEX WITH COPPER,
RP   FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   109-GLU-ASP-110.
RX   PubMed=10220581; DOI=10.1093/oxfordjournals.jbchem.a022366;
RA   Sugawara H., Inoue T., Li C., Gotowda M., Hibino T., Takabe T., Kai Y.;
RT   "Crystal structures of wild-type and mutant plastocyanins from a higher
RT   plant, Silene.";
RL   J. Biochem. 125:899-903(1999).
CC   -!- FUNCTION: Participates in electron transfer between P700 and the
CC       cytochrome b6-f complex in photosystem I.
CC       {ECO:0000269|PubMed:10220581}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000269|PubMed:10220581};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:10220581}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:10220581}; Lumenal side
CC       {ECO:0000269|PubMed:10220581}. Note=Loosely bound to the inner
CC       thylakoid membrane surface in chloroplasts (PubMed:10220581).
CC   -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR   EMBL; X02965; CAA26709.1; -; mRNA.
DR   PIR; A24404; CUQH.
DR   PDB; 1BYO; X-ray; 2.00 A; A/B=67-165.
DR   PDB; 1BYP; X-ray; 1.75 A; A=67-165.
DR   PDBsum; 1BYO; -.
DR   PDBsum; 1BYP; -.
DR   AlphaFoldDB; P07030; -.
DR   SMR; P07030; -.
DR   EvolutionaryTrace; P07030; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   CDD; cd04219; Plastocyanin; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR001235; Copper_blue_Plastocyanin.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR002387; Plastocyanin.
DR   Pfam; PF00127; Copper-bind; 1.
DR   PRINTS; PR00156; COPPERBLUE.
DR   PRINTS; PR00157; PLASTOCYANIN.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR02656; cyanin_plasto; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Copper; Electron transport; Membrane;
KW   Metal-binding; Plastid; Thylakoid; Transit peptide; Transport.
FT   TRANSIT         1..66
FT                   /note="Chloroplast"
FT   CHAIN           67..165
FT                   /note="Plastocyanin, chloroplastic"
FT                   /id="PRO_0000002896"
FT   DOMAIN          67..165
FT                   /note="Plastocyanin-like"
FT   BINDING         103
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:10220581"
FT   BINDING         150
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:10220581"
FT   BINDING         153
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:10220581"
FT   BINDING         158
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:10220581"
FT   MUTAGEN         109..110
FT                   /note="ED->KK: Decreased rate of electron transfer."
FT                   /evidence="ECO:0000269|PubMed:10220581"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:1BYP"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1BYO"
FT   STRAND          79..88
FT                   /evidence="ECO:0007829|PDB:1BYP"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:1BYP"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:1BYO"
FT   HELIX           118..121
FT                   /evidence="ECO:0007829|PDB:1BYP"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:1BYP"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:1BYP"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:1BYP"
FT   TURN            154..157
FT                   /evidence="ECO:0007829|PDB:1BYP"
FT   STRAND          159..165
FT                   /evidence="ECO:0007829|PDB:1BYP"
SQ   SEQUENCE   165 AA;  16620 MW;  C4F817E69BC514A0 CRC64;
     MATVTSSAAV AIPSFAGLKA SSTTRAATVK VAVATPRMSI KASLKDVGVV VAATAAAGIL
     AGNAMAAEVL LGSSDGGLAF VPSDLSIASG EKITFKNNAG FPHNVVFDED EVPAGVDVTK
     ISMPEEDLLN APGEEYSVTL TEKGTYKFYC APHAGAGMVG KVTVN