PLAS2_POPNI
ID PLAS2_POPNI Reviewed; 168 AA.
AC P11970;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Plastocyanin B, chloroplastic;
DE Short=PCb;
DE Flags: Precursor;
GN Name=PETE;
OS Populus nigra (Lombardy poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3691;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Italica; TISSUE=Leaf;
RA Reichert J., Jenzelewski V., Haehnel W.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 70-168, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Italica;
RA Dimitrov M.I., Egorov C.A., Donchev A.A., Atanasov B.P.;
RT "Complete amino acid sequence of poplar plastocyanin b.";
RL FEBS Lett. 226:17-22(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 70-168 IN COMPLEX WITH COPPER,
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Italica;
RX PubMed=22883960; DOI=10.1016/j.jinorgbio.2012.07.015;
RA Kachalova G.S., Shosheva A.C., Bourenkov G.P., Donchev A.A., Dimitrov M.I.,
RA Bartunik H.D.;
RT "Structural comparison of the poplar plastocyanin isoforms PCa and PCb
RT sheds new light on the role of the copper site geometry in interactions
RT with redox partners in oxygenic photosynthesis.";
RL J. Inorg. Biochem. 115:174-181(2012).
CC -!- FUNCTION: Participates in electron transfer between P700 and the
CC cytochrome b6-f complex in photosystem I.
CC {ECO:0000269|PubMed:22883960}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:22883960};
CC Note=The crystal structure with reduced Cu(1+) has also been determined
CC (PubMed:22883960).;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:22883960, ECO:0000269|Ref.2}; Peripheral membrane
CC protein {ECO:0000269|PubMed:22883960}; Lumenal side
CC {ECO:0000269|PubMed:22883960}. Note=Loosely bound to the inner
CC thylakoid membrane surface in chloroplasts (PubMed:22883960).
CC -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000305}.
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DR EMBL; Z50186; CAA90565.1; -; mRNA.
DR PIR; S00210; S00210.
DR PIR; S58208; S58208.
DR PDB; 4DP0; X-ray; 1.50 A; X=70-168.
DR PDB; 4DP1; X-ray; 1.35 A; X=70-168.
DR PDB; 4DP2; X-ray; 1.80 A; X=70-168.
DR PDB; 4DP4; X-ray; 1.54 A; X=70-168.
DR PDB; 4DP5; X-ray; 1.88 A; X=70-168.
DR PDB; 4DP6; X-ray; 1.67 A; X=70-168.
DR PDBsum; 4DP0; -.
DR PDBsum; 4DP1; -.
DR PDBsum; 4DP2; -.
DR PDBsum; 4DP4; -.
DR PDBsum; 4DP5; -.
DR PDBsum; 4DP6; -.
DR AlphaFoldDB; P11970; -.
DR SMR; P11970; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd04219; Plastocyanin; 1.
DR Gene3D; 2.60.40.420; -; 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 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; Chloroplast; Copper; Direct protein sequencing;
KW Electron transport; Membrane; Metal-binding; Plastid; Thylakoid;
KW Transit peptide; Transport.
FT TRANSIT 1..69
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 70..168
FT /note="Plastocyanin B, chloroplastic"
FT /id="PRO_0000002894"
FT DOMAIN 70..168
FT /note="Plastocyanin-like"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:22883960"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:22883960"
FT BINDING 156
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:22883960"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:22883960"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4DP1"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:4DP1"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:4DP1"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4DP1"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4DP1"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:4DP1"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4DP1"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:4DP1"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4DP1"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4DP1"
SQ SEQUENCE 168 AA; 16981 MW; F20DA6EA2038AEEA CRC64;
MAAVTSAAVS IPSFTGLKAA SASNAKVSAS AKVSASPLPR LSIKASLKEV GAAVVATAAS
AMIASNAMAV DVLLGADDGS LAFVPSEFSV PAGEKIVFKN NAGFPHNVLF DEDAVPSGVD
VSKISMSEED LLNAKGETFE VALSDKGEYT FYCSPHQGAG MVGKVIVN
