ID   PLAS_NOSS1              Reviewed;         139 AA.
AC   P46444;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Plastocyanin;
DE   Flags: Precursor;
GN   Name=petE; OrderedLocusNames=all0258;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8025680; DOI=10.1099/13500872-140-5-1151;
RA   Ghassemian M., Wong B., Ferreira F., Markley J.L., Straus N.A.;
RT   "Cloning, sequencing and transcriptional studies of the genes for
RT   cytochrome c-553 and plastocyanin from Anabaena sp. PCC 7120.";
RL   Microbiology 140:1151-1159(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [3]
RP   STRUCTURE BY NMR OF 35-139 IN COMPLEX WITH COPPER, COFACTOR, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15705583; DOI=10.1074/jbc.m413298200;
RA   Diaz-Moreno I., Diaz-Quintana A., De la Rosa M.A., Ubbink M.;
RT   "Structure of the complex between plastocyanin and cytochrome f from the
RT   cyanobacterium Nostoc sp. PCC 7119 as determined by paramagnetic NMR. The
RT   balance between electrostatic and hydrophobic interactions within the
RT   transient complex determines the relative orientation of the two
RT   proteins.";
RL   J. Biol. Chem. 280:18908-18915(2005).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 35-139 IN COMPLEX WITH COPPER.
RA   Fields B.A., Duff A.P., Govinderaju K., Jackman M.P., Lee H.W.,
RA   Church W.B., Guss J.M., Sykes A.G., Freeman H.C.;
RT   "The crystal structure and electron-transfer reactivity of plastocyanin
RT   from a cyanobacterium, Anabaena variabilis.";
RL   Submitted (MAR-2006) to the PDB data bank.
CC   -!- FUNCTION: Participates in electron transfer between P700 and the
CC       cytochrome b6-f complex in photosystem I.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00566,
CC         ECO:0000269|PubMed:15705583, ECO:0000269|Ref.4};
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00566, ECO:0000269|PubMed:15705583}; Peripheral membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_00566, ECO:0000269|PubMed:15705583};
CC       Lumenal side {ECO:0000255|HAMAP-Rule:MF_00566,
CC       ECO:0000269|PubMed:15705583}. Note=Loosely bound to the thylakoid inner
CC       membrane surface.
CC   -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00566}.
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DR   EMBL; L19417; AAA59364.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB77782.1; -; Genomic_DNA.
DR   PIR; AB1839; AB1839.
DR   PIR; I39614; I39614.
DR   RefSeq; WP_010994435.1; NZ_RSCN01000032.1.
DR   PDB; 1TU2; NMR; -; A=35-139.
DR   PDB; 2CJ3; X-ray; 1.70 A; A/B=35-139.
DR   PDBsum; 1TU2; -.
DR   PDBsum; 2CJ3; -.
DR   AlphaFoldDB; P46444; -.
DR   BMRB; P46444; -.
DR   SMR; P46444; -.
DR   STRING; 103690.17135236; -.
DR   TCDB; 3.D.3.5.6; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR   EnsemblBacteria; BAB77782; BAB77782; BAB77782.
DR   KEGG; ana:all0258; -.
DR   eggNOG; COG3794; Bacteria.
DR   OMA; YDYYCEP; -.
DR   OrthoDB; 1654242at2; -.
DR   EvolutionaryTrace; P46444; -.
DR   Proteomes; UP000002483; Chromosome.
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   3D-structure; Copper; Electron transport; Membrane; Metal-binding;
KW   Reference proteome; Signal; Thylakoid; Transport.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000250"
FT   CHAIN           35..139
FT                   /note="Plastocyanin"
FT                   /id="PRO_0000002899"
FT   DOMAIN          35..139
FT                   /note="Plastocyanin-like"
FT   BINDING         73
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15705583, ECO:0000269|Ref.4"
FT   BINDING         123
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15705583, ECO:0000269|Ref.4"
FT   BINDING         126
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15705583, ECO:0000269|Ref.4"
FT   BINDING         131
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:15705583, ECO:0000269|Ref.4"
FT   STRAND          36..42
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   STRAND          48..57
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   HELIX           87..93
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   STRAND          116..122
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:2CJ3"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:2CJ3"
SQ   SEQUENCE   139 AA;  14619 MW;  17BE99202F8B796E CRC64;
     MKLIAASLRR LSLAVLTVLL VVSSFAVFTP SASAETYTVK LGSDKGLLVF EPAKLTIKPG
     DTVEFLNNKV PPHNVVFDAA LNPAKSADLA KSLSHKQLLM SPGQSTSTTF PADAPAGEYT
     FYCEPHRGAG MVGKITVAG