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PLAS_SYNY3
ID   PLAS_SYNY3              Reviewed;         126 AA.
AC   P21697;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Plastocyanin;
DE   Flags: Precursor;
GN   Name=petE; OrderedLocusNames=sll0199;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY COPPER.
RX   PubMed=2129338; DOI=10.1007/bf00017837;
RA   Briggs L.M., Pecoraro V.L., McIntosh L.;
RT   "Copper-induced expression, cloning, and regulatory studies of the
RT   plastocyanin gene from the cyanobacterium Synechocystis sp. PCC 6803.";
RL   Plant Mol. Biol. 15:633-642(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 29-47.
RX   PubMed=9298645; DOI=10.1002/elps.1150180806;
RA   Sazuka T., Ohara O.;
RT   "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT   PCC6803: linking 130 protein spots with their respective genes.";
RL   Electrophoresis 18:1252-1258(1997).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 29-126 IN COMPLEX WITH COPPER,
RP   FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX   PubMed=9466912; DOI=10.1006/jmbi.1997.1455;
RA   Romero A., de la Cerda B., Varela P.F., Navarro J.A., Hervas M.,
RA   de la Rosa M.A.;
RT   "The 2.15 A crystal structure of a triple mutant plastocyanin from the
RT   cyanobacterium Synechocystis sp. PCC 6803.";
RL   J. Mol. Biol. 275:327-336(1998).
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:9466912}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00566,
CC         ECO:0000269|PubMed:9466912};
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000269|PubMed:9466912}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:9466912}; Lumenal side
CC       {ECO:0000269|PubMed:9466912}. Note=Loosely bound to the thylakoid inner
CC       membrane surface (PubMed:9466912).
CC   -!- INDUCTION: By copper. {ECO:0000269|PubMed:2129338}.
CC   -!- SIMILARITY: Belongs to the plastocyanin family. {ECO:0000255|HAMAP-
CC       Rule:MF_00566}.
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DR   EMBL; X54105; CAA38038.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA10227.1; -; Genomic_DNA.
DR   PIR; S76375; S76375.
DR   PDB; 1J5C; NMR; -; A=29-126.
DR   PDB; 1J5D; NMR; -; A=29-126.
DR   PDB; 1JXD; NMR; -; A=29-126.
DR   PDB; 1JXF; NMR; -; A=29-126.
DR   PDB; 1M9W; NMR; -; A=29-126.
DR   PDB; 1PCS; X-ray; 2.15 A; A=29-126.
DR   PDBsum; 1J5C; -.
DR   PDBsum; 1J5D; -.
DR   PDBsum; 1JXD; -.
DR   PDBsum; 1JXF; -.
DR   PDBsum; 1M9W; -.
DR   PDBsum; 1PCS; -.
DR   AlphaFoldDB; P21697; -.
DR   BMRB; P21697; -.
DR   SMR; P21697; -.
DR   IntAct; P21697; 2.
DR   STRING; 1148.1001599; -.
DR   PaxDb; P21697; -.
DR   EnsemblBacteria; BAA10227; BAA10227; BAA10227.
DR   KEGG; syn:sll0199; -.
DR   eggNOG; COG3794; Bacteria.
DR   InParanoid; P21697; -.
DR   OMA; YDYYCEP; -.
DR   PhylomeDB; P21697; -.
DR   EvolutionaryTrace; P21697; -.
DR   Proteomes; UP000001425; 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   1: Evidence at protein level;
KW   3D-structure; Copper; Direct protein sequencing; Electron transport;
KW   Membrane; Metal-binding; Reference proteome; Signal; Thylakoid; Transport.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:9298645"
FT   CHAIN           29..126
FT                   /note="Plastocyanin"
FT                   /id="PRO_0000002904"
FT   DOMAIN          29..126
FT                   /note="Plastocyanin-like"
FT   BINDING         67
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:9466912"
FT   BINDING         111
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:9466912"
FT   BINDING         114
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:9466912"
FT   BINDING         119
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:9466912"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:1J5C"
FT   STRAND          42..52
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:1J5D"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   HELIX           78..84
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   TURN            115..118
FT                   /evidence="ECO:0007829|PDB:1PCS"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:1PCS"
SQ   SEQUENCE   126 AA;  13146 MW;  BA4E48109145C9EA CRC64;
     MSKKFLTILA GLLLVVSSFF LSVSPAAAAN ATVKMGSDSG ALVFEPSTVT IKAGEEVKWV
     NNKLSPHNIV FAADGVDADT AAKLSHKGLA FAAGESFTST FTEPGTYTYY CEPHRGAGMV
     GKVVVE
 
 
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