CPCL_NOSS1
ID CPCL_NOSS1 Reviewed; 237 AA.
AC P29988;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Photosystem I-associated linker protein CpcL {ECO:0000303|PubMed:24550276};
DE AltName: Full=L-RC 27.2;
DE AltName: Full=Phycobilisome rod-core linker polypeptide CpcG3 {ECO:0000303|PubMed:1743523};
GN Name=cpcL {ECO:0000303|PubMed:24550276};
GN Synonyms=cpcG3 {ECO:0000303|PubMed:1743523}; OrderedLocusNames=alr0536;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=1743523; DOI=10.1016/0378-1119(91)90301-q;
RA Bryant D.A., Stirewalt V.L., Glauser M., Frank G., Sidler W., Zuber H.;
RT "A small multigene family encodes the rod-core linker polypeptides of
RT Anabaena sp. PCC7120 phycobilisomes.";
RL Gene 107:91-99(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-16, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=24550276; DOI=10.1073/pnas.1320599111;
RA Watanabe M., Semchonok D.A., Webber-Birungi M.T., Ehira S., Kondo K.,
RA Narikawa R., Ohmori M., Boekema E.J., Ikeuchi M.;
RT "Attachment of phycobilisomes in an antenna-photosystem I supercomplex of
RT cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2512-2517(2014).
CC -!- FUNCTION: Rod linker protein, associated with phycocyanin (PC). Linker
CC polypeptides determine the state of aggregation and the location of the
CC disk-shaped phycobiliprotein units within the phycobilisome (PBS) and
CC modulate their spectroscopic properties in order to mediate a directed
CC and optimal energy transfer. Forms a supercomplex with tetrameric
CC photosystem I (PSI) and PC that allows efficient energy transfer from
CC PC to PSI. This protein seems to be in the middle of the PC hexameric
CC rod and may anchor the PC rods at the periphery of PSI tetramers. May
CC be involved in the cyclic electron transport around PSI that provides
CC ATP needed for N(2) fixation in heterocysts (PubMed:24550276).
CC {ECO:0000269|PubMed:24550276}.
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). In vegetative cells associated
CC substoichiometrically with photosystem I and phycobiliproteins
CC phycocyanin as well as phycoerythrocyanin in the thylakoid membrane,
CC not found in conventional, hemidiscoidal phycobilisomes.
CC {ECO:0000269|PubMed:24550276}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:24550276}; Single-pass membrane protein
CC {ECO:0000255}. Note=Part of a core-less phycobilisome rod (CpcL-PBS). A
CC portion of the protein is not associated with thylakoids in N(2)-fixing
CC heterocysts. {ECO:0000269|PubMed:24550276}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both vegetative cells and in N(2)-
CC fixing heterocysts; considerably more abundant in heterocysts (at
CC protein level). {ECO:0000269|PubMed:24550276}.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; M80435; AAA22038.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB72494.1; -; Genomic_DNA.
DR PIR; AG1873; AG1873.
DR PIR; JS0594; JS0594.
DR RefSeq; WP_010994712.1; NZ_RSCN01000059.1.
DR AlphaFoldDB; P29988; -.
DR SMR; P29988; -.
DR STRING; 103690.17129881; -.
DR EnsemblBacteria; BAB72494; BAB72494; BAB72494.
DR KEGG; ana:alr0536; -.
DR eggNOG; COG0237; Bacteria.
DR OMA; TDRPFSF; -.
DR OrthoDB; 1021247at2; -.
DR Proteomes; UP000002483; 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: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 Antenna complex; Direct protein sequencing; Membrane; Photosynthesis;
KW Phycobilisome; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:24550276"
FT CHAIN 2..237
FT /note="Photosystem I-associated linker protein CpcL"
FT /id="PRO_0000199246"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 11..191
FT /note="PBS-linker"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
SQ SEQUENCE 237 AA; 27206 MW; 049FE01DD5BF8355 CRC64;
MALPLLEYKP TTQNQRVQSF GTADVNEDTP YIYRLENANS PSEIEELIWA AYRQVFNEQE
ILKFNRQIGL ETQLKNRSIT VKDFIRGLAK SERFYQLVVT PNNNYRLVEM SLKRLLGRSP
YNEEEKIAWS IQIASKGWGG FVDALIDSTE YEQAFGDNTV PYQRKRLTTD RPFSFTPRYG
ADYRDRAGIV RPGRMSNWNN SANQNYDGVA ILGVLLAISA GMTFLFVLNW LGISSSF
