CPCL_SYNY3
ID CPCL_SYNY3 Reviewed; 249 AA.
AC P74625;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Photosystem I-associated linker protein CpcL {ECO:0000303|PubMed:31015331};
DE AltName: Full=Phycobilisome rod-core linker polypeptide CpcG2 {ECO:0000303|PubMed:16049785};
GN Name=cpcL {ECO:0000303|PubMed:31015331};
GN Synonyms=cpcG2 {ECO:0000303|PubMed:16049785}; OrderedLocusNames=sll1471;
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 [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 [2]
RP PROTEIN SEQUENCE OF 2-16, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=31015331; DOI=10.1128/mbio.00669-19;
RA Liu H., Weisz D.A., Zhang M.M., Cheng M., Zhang B., Zhang H.,
RA Gerstenecker G.S., Pakrasi H.B., Gross M.L., Blankenship R.E.;
RT "Phycobilisomes Harbor FNRL in Cyanobacteria.";
RL MBio 10:0-0(2019).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=16049785; DOI=10.1007/s11120-004-7762-9;
RA Kondo K., Geng X.X., Katayama M., Ikeuchi M.;
RT "Distinct roles of CpcG1 and CpcG2 in phycobilisome assembly in the
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL Photosyn. Res. 84:269-273(2005).
RN [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17468217; DOI=10.1104/pp.107.099267;
RA Kondo K., Ochiai Y., Katayama M., Ikeuchi M.;
RT "The membrane-associated CpcG2-phycobilisome in Synechocystis: a new
RT photosystem I antenna.";
RL Plant Physiol. 144:1200-1210(2007).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=19152018; DOI=10.1007/s11120-008-9399-6;
RA Kondo K., Mullineaux C.W., Ikeuchi M.;
RT "Distinct roles of CpcG1-phycobilisome and CpcG2-phycobilisome in state
RT transitions in a cyanobacterium Synechocystis sp. PCC 6803.";
RL Photosyn. Res. 99:217-225(2009).
CC -!- FUNCTION: Rod linker protein, associated with phycocyanin. Linker
CC polypeptides determine the state of aggregation and the location of the
CC disk-shaped phycobiliprotein units within the phycobilisome and
CC modulate their spectroscopic properties in order to mediate a directed
CC and optimal energy transfer. Plays a role in energy transfer from the
CC phycobilisome to photosystem I (PSI). Although able to transfer energy
CC to both photosystems, this is predominantly a PSI antenna
CC (PubMed:16049785, PubMed:17468217, PubMed:19152018).
CC {ECO:0000269|PubMed:16049785, ECO:0000269|PubMed:17468217,
CC ECO:0000269|PubMed:19152018}.
CC -!- SUBUNIT: Part of a specialized phycobilisome (PBS), a structure that is
CC usually composed of two distinct substructures: a core complex and a
CC number of rods radiating from the core. This protein is part of a core-
CC less PBS rod (called CpcL-PBS) with on average 5 stacked phycocyanin
CC hexamers (PC, CpcA and CpcB). Linker CpcL connects the PC stack to the
CC thylakoid, the hexamers are linked by 1 copy of CpcC1, 3 copies of
CC CpcC2 and the stack is terminated by a single copy of CpcD.
CC Ferredoxin--NADP reductase (petH) is also part of the complex. CpcL-PBS
CC has no central core proteins (allophycocyanin ApcA, ApcB) nor
CC phycobiliprotein ApcE. {ECO:0000269|PubMed:16049785,
CC ECO:0000269|PubMed:17468217, ECO:0000269|PubMed:31015331}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:17468217}; Single-pass membrane protein
CC {ECO:0000255}. Note=Unlike the major phycobilisome supercomplex, this
CC protein is tightly associated with the thylakoid membrane
CC (PubMed:17468217). Part of the PBS rod (PubMed:16049785,
CC PubMed:17468217, PubMed:31015331). {ECO:0000269|PubMed:16049785,
CC ECO:0000269|PubMed:17468217, ECO:0000269|PubMed:31015331}.
CC -!- DISRUPTION PHENOTYPE: No visible growth phenotype, decreased energy
CC transfer to photosystem I. Decreased accumulation of phycocyanin (PC),
CC but no major effects on the phycobilisome supercomplex. A double
CC cpcG1/cpcG2 deletion has even less PC (PubMed:16049785,
CC PubMed:17468217). No change in state 2 to state 1 transitions (i.e.
CC energy transfer to PSII) (PubMed:19152018).
CC {ECO:0000269|PubMed:16049785, ECO:0000269|PubMed:17468217,
CC ECO:0000269|PubMed:19152018}.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000022; BAA18734.1; -; Genomic_DNA.
DR PIR; S76822; S76822.
DR AlphaFoldDB; P74625; -.
DR SMR; P74625; -.
DR IntAct; P74625; 4.
DR STRING; 1148.1653823; -.
DR PaxDb; P74625; -.
DR EnsemblBacteria; BAA18734; BAA18734; BAA18734.
DR KEGG; syn:sll1471; -.
DR eggNOG; COG0448; Bacteria.
DR OMA; TDRPFSF; -.
DR PhylomeDB; P74625; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:InterPro.
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 Antenna complex; Direct protein sequencing; Membrane; Phycobilisome;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:31015331"
FT CHAIN 2..249
FT /note="Photosystem I-associated linker protein CpcL"
FT /id="PRO_0000449925"
FT TRANSMEM 223..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 11..189
FT /note="PBS-linker"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
SQ SEQUENCE 249 AA; 28523 MW; 83C568AFB3173C1A CRC64;
MTLPLIAYAP VSQNQRVTNY EVSGDEHARI FTTEGTLSPS AMDNLIAAAY RQVFNEQQMI
QSNRQIALES QFKNQQITVR DFIRGLALSD SFRRRNFEVN NNYRFVQMCI QRLLGRDVYS
EEEKIAWSIV IATKGLPGFI NELLNSQEYL ENFGYDTVPY QRRRILPQRI SGELPFARMP
RYGADHREKL EAIGYFRNQA PLTYRWEWQK QPYPAGVYLA GKVVLYVGGA LVSLGIIAVA
LSAWGIIGL
