PLAS_PHOLA
ID PLAS_PHOLA Reviewed; 139 AA.
AC Q51883;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Plastocyanin;
DE Flags: Precursor;
GN Name=petE;
OS Phormidium laminosum.
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=32059;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7865788; DOI=10.1007/bf00019189;
RA Varley J.P.A., Moehrle J.J., Manasse R.S., Bendall D.S., Howe C.J.;
RT "Characterization of plastocyanin from the cyanobacterium Phormidium
RT laminosum: copper-inducible expression and SecA-dependent targeting in
RT Escherichia coli.";
RL Plant Mol. Biol. 27:179-190(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-139 IN COMPLEX WITH COPPER,
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=10089349; DOI=10.1107/s0907444998012074;
RA Bond C.S., Bendall D.S., Freeman H.C., Guss J.M., Howe C.J., Wagner M.J.,
RA Wilce M.C.;
RT "The structure of plastocyanin from the cyanobacterium Phormidium
RT laminosum.";
RL Acta Crystallogr. D 55:414-421(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:10089349}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00566,
CC ECO:0000269|PubMed:10089349};
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:10089349}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10089349}; Lumenal side
CC {ECO:0000269|PubMed:10089349}. Note=Loosely bound to the thylakoid
CC inner membrane surface (PubMed:10089349).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000255|HAMAP-
CC Rule:MF_00566}.
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DR EMBL; X83207; CAA58210.1; -; Genomic_DNA.
DR PIR; S51922; S51922.
DR PDB; 1BAW; X-ray; 2.80 A; A/B/C=35-139.
DR PDB; 2Q5B; X-ray; 1.45 A; A/B/C=35-139.
DR PDB; 2W88; X-ray; 2.89 A; A/B/C=35-139.
DR PDB; 2W8C; X-ray; 1.80 A; A/B=35-139.
DR PDB; 3BQV; X-ray; 1.50 A; A=35-139.
DR PDB; 3CVB; X-ray; 1.40 A; A/B=35-139.
DR PDB; 3CVC; X-ray; 1.72 A; A=35-139.
DR PDB; 3CVD; X-ray; 1.50 A; A/B/C=35-139.
DR PDB; 4R0O; X-ray; 4.20 A; A/B/C/D=35-139.
DR PDBsum; 1BAW; -.
DR PDBsum; 2Q5B; -.
DR PDBsum; 2W88; -.
DR PDBsum; 2W8C; -.
DR PDBsum; 3BQV; -.
DR PDBsum; 3CVB; -.
DR PDBsum; 3CVC; -.
DR PDBsum; 3CVD; -.
DR PDBsum; 4R0O; -.
DR AlphaFoldDB; Q51883; -.
DR SASBDB; Q51883; -.
DR SMR; Q51883; -.
DR EvolutionaryTrace; Q51883; -.
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; Direct protein sequencing; Electron transport;
KW Membrane; Metal-binding; Signal; Thylakoid; Transport.
FT SIGNAL 1..34
FT CHAIN 35..139
FT /note="Plastocyanin"
FT /id="PRO_0000002901"
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:10089349"
FT BINDING 123
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10089349"
FT BINDING 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10089349"
FT BINDING 131
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10089349"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:3CVB"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3CVC"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3CVB"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:3CVB"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1BAW"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3CVB"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2Q5B"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3CVB"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:3CVB"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:3CVB"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3CVB"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3CVB"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3CVB"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3CVB"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3CVB"
SQ SEQUENCE 139 AA; 14909 MW; 87989D943B28F951 CRC64;
MKLIAQISRS LSLALFALVL MVGSFVAVMS PAAAETFTVK MGADSGLLQF EPANVTVHPG
DTVKWVNNKL PPHNILFDDK QVPGASKELA DKLSHSQLMF SPGESYEITF SSDFPAGTYT
YYCAPHRGAG MVGKITVEG
