PLAS_GLOC7
ID PLAS_GLOC7 Reviewed; 127 AA.
AC B7KAE8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Plastocyanin {ECO:0000255|HAMAP-Rule:MF_00566};
DE Flags: Precursor;
GN Name=petE {ECO:0000255|HAMAP-Rule:MF_00566};
GN OrderedLocusNames=PCC7424_4559;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001291; ACK72922.1; -; Genomic_DNA.
DR RefSeq; WP_015956505.1; NC_011729.1.
DR AlphaFoldDB; B7KAE8; -.
DR SMR; B7KAE8; -.
DR STRING; 65393.PCC7424_4559; -.
DR EnsemblBacteria; ACK72922; ACK72922; PCC7424_4559.
DR KEGG; cyc:PCC7424_4559; -.
DR eggNOG; COG3794; Bacteria.
DR HOGENOM; CLU_084115_0_1_3; -.
DR OMA; YDYYCEP; -.
DR OrthoDB; 1654242at2; -.
DR Proteomes; UP000002384; 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..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT CHAIN 29..127
FT /note="Plastocyanin"
FT /id="PRO_5000418167"
FT DOMAIN 29..127
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT BINDING 67
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT BINDING 112
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00566"
FT BINDING 115
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"
SQ SEQUENCE 127 AA; 13681 MW; 5C74C17618CD44C3 CRC64;
MLKKLGVLLS AIVLVIASFF VTVTPALAET YTVKMGSDQG LLKFDPPQLT IKAGDTVKWV
NNKLAPHNAV FDNSKVPDSV SATKISHKAL VFSPGESFTT TFDEPGTYTY YCEPHRGAGM
VGTITVE