ID   PLAS_PROHO              Reviewed;         131 AA.
AC   P50057;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=Plastocyanin;
DE   Flags: Precursor;
GN   Name=petE;
OS   Prochlorothrix hollandica.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Prochlorotrichales;
OC   Prochlorotrichaceae; Prochlorothrix.
OX   NCBI_TaxID=1223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ACC 15-2;
RX   PubMed=7803460; DOI=10.1016/0005-2728(94)90069-8;
RA   Arudchandran A., Seeburg D., Burkhart W., Bullerjahn G.S.;
RT   "Nucleotide sequence of the petE gene encoding plastocyanin from the
RT   photosynthetic prokaryote, Prochlorothrix hollandica.";
RL   Biochim. Biophys. Acta 1188:447-449(1994).
RN   [2]
RP   STRUCTURE BY NMR OF 35-131, SEQUENCE REVISION TO 95, FUNCTION, COFACTOR,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=10213601; DOI=10.1021/bi983024f;
RA   Babu C.R., Volkman B.F., Bullerjahn G.S.;
RT   "NMR solution structure of plastocyanin from the photosynthetic prokaryote,
RT   Prochlorothrix hollandica.";
RL   Biochemistry 38:4988-4995(1999).
CC   -!- FUNCTION: Participates in electron transfer between P700 and the
CC       cytochrome b6-f complex in photosystem I. {ECO:0000255|HAMAP-
CC       Rule:MF_00566, ECO:0000269|PubMed:10213601}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00566, ECO:0000269|PubMed:10213601};
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000269|PubMed:10213601}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:10213601}; Lumenal side
CC       {ECO:0000269|PubMed:10213601}. Note=Loosely bound to the thylakoid
CC       inner membrane surface (PubMed:10213601).
CC   -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00566}.
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DR   EMBL; U13912; AAD09144.1; -; Genomic_DNA.
DR   PIR; A44637; A44637.
DR   PDB; 1B3I; NMR; -; A=35-131.
DR   PDB; 2B3I; NMR; -; A=35-131.
DR   PDB; 2JXM; NMR; -; A=35-131.
DR   PDBsum; 1B3I; -.
DR   PDBsum; 2B3I; -.
DR   PDBsum; 2JXM; -.
DR   AlphaFoldDB; P50057; -.
DR   BMRB; P50057; -.
DR   SMR; P50057; -.
DR   EvolutionaryTrace; P50057; -.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04219; Plastocyanin; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   HAMAP; MF_00566; Cytb6_f_plastocyanin; 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   InterPro; IPR023511; Plastocyanin_cyanobac.
DR   NCBIfam; TIGR02656; cyanin_plasto; 1.
DR   PANTHER; PTHR34192; PLASTOCYANIN MAJOR ISOFORM, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR34192:SF10; PLASTOCYANIN MAJOR ISOFORM, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00127; Copper-bind; 1.
DR   PRINTS; PR00156; COPPERBLUE.
DR   PRINTS; PR00157; PLASTOCYANIN.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Electron transport; Membrane; Metal-binding; Signal;
KW   Thylakoid; Transport.
FT   SIGNAL          1..34
FT   CHAIN           35..131
FT                   /note="Plastocyanin"
FT                   /id="PRO_0000002902"
FT   DOMAIN          35..131
FT                   /note="Plastocyanin-like"
FT   BINDING         73
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000305"
FT   BINDING         116
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000305"
FT   BINDING         119
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000305"
FT   BINDING         124
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT   CONFLICT        95
FT                   /note="A -> R (in Ref. 1; AAD09144)"
FT                   /evidence="ECO:0000305"
FT   STRAND          37..43
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   STRAND          47..57
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:2B3I"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:2B3I"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   TURN            119..123
FT                   /evidence="ECO:0007829|PDB:1B3I"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:1B3I"
SQ   SEQUENCE   131 AA;  13613 MW;  72872020BB7326D0 CRC64;
     MKFFASLSKR FAPVLSLVVL VAGTLLLSAA PASAATVQIK MGTDKYAPLY EPKALSISAG
     DTVEFVMNKV GPHNVIFDKV PAGESAPALS NTKLAIAPGS FYSVTLGTPG TYSFYCTPHR
     GAGMVGTITV E
//