ID   PLAS_NOSSO              Reviewed;         139 AA.
AC   O52830;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Plastocyanin;
DE   Flags: Precursor;
GN   Name=petE;
OS   Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1168;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9473522; DOI=10.1006/bbrc.1997.7953;
RA   Molina-Heredia F.P., Hervas M., Navarro J.A., De la Rosa M.A.;
RT   "Cloning and correct expression in Escherichia coli of the petE and petJ
RT   genes respectively encoding plastocyanin and cytochrome c6 from the
RT   cyanobacterium Anabaena sp. PCC 7119.";
RL   Biochem. Biophys. Res. Commun. 243:302-306(1998).
RN   [2]
RP   SEQUENCE REVISION TO 132.
RA   Molina-Heredia F.P.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00566};
CC   -!- INTERACTION:
CC       O52830; Q6H8M0: petA; NbExp=2; IntAct=EBI-701517, EBI-701525;
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00566}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00566}; Lumenal side {ECO:0000255|HAMAP-Rule:MF_00566}.
CC       Note=Loosely bound to the thylakoid inner membrane surface.
CC   -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00566}.
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DR   EMBL; AJ002362; CAA05338.2; -; Genomic_DNA.
DR   AlphaFoldDB; O52830; -.
DR   BMRB; O52830; -.
DR   SMR; O52830; -.
DR   IntAct; O52830; 1.
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; -; 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   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   Copper; Electron transport; Membrane; Metal-binding; Signal; Thylakoid;
KW   Transport.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000250"
FT   CHAIN           35..139
FT                   /note="Plastocyanin"
FT                   /id="PRO_0000002898"
FT   DOMAIN          35..139
FT                   /note="Plastocyanin-like"
FT   BINDING         73
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT   BINDING         123
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT   BINDING         126
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT   BINDING         131
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
SQ   SEQUENCE   139 AA;  14619 MW;  17BE99202F8B796E CRC64;
     MKLIAASLRR LSLAVLTVLL VVSSFAVFTP SASAETYTVK LGSDKGLLVF EPAKLTIKPG
     DTVEFLNNKV PPHNVVFDAA LNPAKSADLA KSLSHKQLLM SPGQSTSTTF PADAPAGEYT
     FYCEPHRGAG MVGKITVAG