PLAS_SYNJB
ID PLAS_SYNJB Reviewed; 136 AA.
AC Q2JHE1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Plastocyanin {ECO:0000255|HAMAP-Rule:MF_00566};
DE Flags: Precursor;
GN Name=petE {ECO:0000255|HAMAP-Rule:MF_00566}; OrderedLocusNames=CYB_1803;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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 -!- 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; CP000240; ABD02760.1; -; Genomic_DNA.
DR RefSeq; WP_011433401.1; NC_007776.1.
DR AlphaFoldDB; Q2JHE1; -.
DR SMR; Q2JHE1; -.
DR STRING; 321332.CYB_1803; -.
DR KEGG; cyb:CYB_1803; -.
DR eggNOG; COG3794; Bacteria.
DR HOGENOM; CLU_084115_0_1_3; -.
DR OMA; YDYYCEP; -.
DR OrthoDB; 1654242at2; -.
DR Proteomes; UP000001938; 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 3: Inferred from homology;
KW Copper; Electron transport; Membrane; Metal-binding; Reference proteome;
KW Signal; Thylakoid; Transport.
FT SIGNAL 1..34
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT CHAIN 35..136
FT /note="Plastocyanin"
FT /id="PRO_1000146803"
FT DOMAIN 35..136
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT BINDING 73
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT BINDING 120
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 128
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
SQ SEQUENCE 136 AA; 14523 MW; 79067ED519C15029 CRC64;
MSLVFNLVKR LQLILLSLVV GGLAVAFLSN PAAAETYIVK MGSDKAQLVY DPPSLTINQG
DTVQWVNNKV YPHNVVFDKV PGGDAALAAK LSHKALLTAP KQVVESAFVD VPPGEYTYYC
TPHRGAGMVG KIIVNG
