PLAS_SYNE7
ID PLAS_SYNE7 Reviewed; 125 AA.
AC P55020; Q31PA1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Plastocyanin;
DE Flags: Precursor;
GN Name=petE; OrderedLocusNames=Synpcc7942_1088;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8759846; DOI=10.1128/jb.178.16.4839-4846.1996;
RA Eriksson M.J., Clarke A.K.;
RT "The heat shock protein ClpB mediates the development of thermotolerance in
RT the cyanobacterium Synechococcus sp. strain PCC 7942.";
RL J. Bacteriol. 178:4839-4846(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 35-125 IN COMPLEX WITH COPPER,
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=10320332; DOI=10.1021/bi9824442;
RA Inoue T., Sugawara H., Hamanaka S., Tsukui H., Suzuki E., Kohzuma T.,
RA Kai Y.;
RT "Crystal structure determinations of oxidized and reduced plastocyanin from
RT the cyanobacterium Synechococcus sp. PCC 7942.";
RL Biochemistry 38:6063-6069(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:10320332}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00566,
CC ECO:0000269|PubMed:10320332};
CC Note=The crystal structure with reduced Cu(1+) has also been determined
CC (PubMed:10320332).;
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:10320332}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10320332}; Lumenal side
CC {ECO:0000269|PubMed:10320332}. Note=Loosely bound to the thylakoid
CC inner membrane surface (PubMed:10320332).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000255|HAMAP-
CC Rule:MF_00566}.
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DR EMBL; U20147; AAB65803.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57118.1; -; Genomic_DNA.
DR RefSeq; WP_011242773.1; NC_007604.1.
DR PDB; 1BXU; X-ray; 1.90 A; A=35-125.
DR PDB; 1BXV; X-ray; 1.80 A; A=35-125.
DR PDBsum; 1BXU; -.
DR PDBsum; 1BXV; -.
DR AlphaFoldDB; P55020; -.
DR SMR; P55020; -.
DR STRING; 1140.Synpcc7942_1088; -.
DR PRIDE; P55020; -.
DR EnsemblBacteria; ABB57118; ABB57118; Synpcc7942_1088.
DR KEGG; syf:Synpcc7942_1088; -.
DR eggNOG; COG3794; Bacteria.
DR HOGENOM; CLU_084115_0_1_3; -.
DR OMA; YDYYCEP; -.
DR OrthoDB; 1654242at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_1088-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_1088-MON; -.
DR EvolutionaryTrace; P55020; -.
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; Signal;
KW Thylakoid; Transport.
FT SIGNAL 1..34
FT CHAIN 35..125
FT /note="Plastocyanin"
FT /id="PRO_0000002903"
FT DOMAIN 35..125
FT /note="Plastocyanin-like"
FT BINDING 73
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10320332"
FT BINDING 110
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10320332"
FT BINDING 113
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10320332"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10320332"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1BXV"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:1BXV"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1BXV"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1BXV"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1BXV"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1BXV"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1BXV"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1BXV"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1BXV"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1BXV"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1BXV"
SQ SEQUENCE 125 AA; 13308 MW; 537DC77B6743A33D CRC64;
MKVLASFARR LSLFAVAAVL CVGSFFLSAA PASAQTVAIK MGADNGMLAF EPSTIEIQAG
DTVQWVNNKL APHNVVVEGQ PELSHKDLAF SPGETFEATF SEPGTYTYYC EPHRGAGMVG
KIVVQ
