PYG1_SYNP2
ID PYG1_SYNP2 Reviewed; 248 AA.
AC Q05238; B1XIE4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Phycobilisome rod-core linker polypeptide CpcG;
DE AltName: Full=L-RC 28.5;
GN Name=cpcG; OrderedLocusNames=SYNPCC7002_A0811;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bryant D.A.;
RT "Cyanobacterial phycobilisomes: progress towards a complete structural and
RT functional analysis via molecular genetics.";
RL (In) Bogorad L., Vasil I.K. (eds.);
RL Cell culture and somatic cell genetics of plants, pp.7B:255-298, Academic
RL Press, New York (1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-23.
RX PubMed=2164365; DOI=10.1007/bf00245264;
RA Bryant D.A., de Lorimier R., Guglielmi G., Stevens S.E. Jr.;
RT "Structural and compositional analyses of the phycobilisomes of
RT Synechococcus sp. PCC 7002. Analyses of the wild-type strain and a
RT phycocyanin-less mutant constructed by interposon mutagenesis.";
RL Arch. Microbiol. 153:550-560(1990).
CC -!- FUNCTION: Rod-core linker protein required for attachment of
CC phycocyanin to allophycocyanin in cores of phycobilisomes.
CC -!- FUNCTION: Linker polypeptides determine the state of aggregation and
CC the location of the disk-shaped phycobiliprotein units within the
CC phycobilisome and modulate their spectroscopic properties in order to
CC mediate a directed and optimal energy transfer.
CC -!- SUBUNIT: The phycobilisome is a hemidiscoidal structure that is
CC composed of two distinct substructures: a core complex and a number of
CC rods radiating from the core.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; CP000951; ACA98815.1; -; Genomic_DNA.
DR RefSeq; WP_012306439.1; NC_010475.1.
DR PDB; 7EXT; EM; 3.50 A; A1/A2/A4/A5/A6/A8=1-248.
DR PDBsum; 7EXT; -.
DR AlphaFoldDB; Q05238; -.
DR SMR; Q05238; -.
DR STRING; 32049.SYNPCC7002_A0811; -.
DR EnsemblBacteria; ACA98815; ACA98815; SYNPCC7002_A0811.
DR KEGG; syp:SYNPCC7002_A0811; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_086930_0_0_3; -.
DR OMA; GFPQIIW; -.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3130.20; -; 1.
DR InterPro; IPR001297; PBS_linker_dom.
DR InterPro; IPR038255; PBS_linker_sf.
DR InterPro; IPR016470; Phycobilisome.
DR Pfam; PF00427; PBS_linker_poly; 1.
DR PIRSF; PIRSF005898; Phycobilisome_CpeC/CpcI; 1.
DR PROSITE; PS51445; PBS_LINKER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Direct protein sequencing; Membrane;
KW Photosynthesis; Phycobilisome; Reference proteome; Thylakoid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2164365"
FT CHAIN 2..248
FT /note="Phycobilisome rod-core linker polypeptide CpcG"
FT /id="PRO_0000199256"
FT DOMAIN 11..188
FT /note="PBS-linker"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
SQ SEQUENCE 248 AA; 28511 MW; EA4C748DB525D064 CRC64;
MTIPLLQYAP SSQNTRVAGY TVGGDEQPFV FTTDNVISDS DFDVLINAAY RQIFFHAFKC
DRQQLLESQL RNGQITVRDF IRGLLLSETF IDSFYNKNSN YRFVEQCIQR VLGRDPFSEQ
EKIAWSIVIC TKGLAAFVDQ LLNTDEYMEN FGYDTVPYQR RRSLASREQG EIPFNIKSPR
YDAYYRSQLG FPQVVWQNAV RRFRTPDRVP QAGDPALFLN MARSAQIPKV NVRVSAADIS
LAAVPYRN