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PYR1_THEVB
ID   PYR1_THEVB              Reviewed;         287 AA.
AC   P50034;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod;
GN   Name=cpcC; OrderedLocusNames=tlr1959;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shimazu T., Soga M., Hirano M., Katoh S.;
RT   "Cloning and sequencing of the phycocyanin operon from the thermophilic
RT   cyanobacterium Synechococcus elongatus.";
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Note=This protein occurs in the rod, it is associated
CC       with phycocyanin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR   EMBL; D13173; BAA02457.1; -; Genomic_DNA.
DR   EMBL; BA000039; BAC09511.1; -; Genomic_DNA.
DR   RefSeq; NP_682749.1; NC_004113.1.
DR   RefSeq; WP_011057794.1; NC_004113.1.
DR   PDB; 2L8V; NMR; -; A=20-153.
DR   PDBsum; 2L8V; -.
DR   AlphaFoldDB; P50034; -.
DR   SMR; P50034; -.
DR   STRING; 197221.22295685; -.
DR   EnsemblBacteria; BAC09511; BAC09511; BAC09511.
DR   KEGG; tel:tlr1959; -.
DR   PATRIC; fig|197221.4.peg.2049; -.
DR   eggNOG; COG0237; Bacteria.
DR   OMA; YNSFQTR; -.
DR   OrthoDB; 920849at2; -.
DR   Proteomes; UP000000440; 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; IPR008213; CpcD-like_dom.
DR   InterPro; IPR001297; PBS_linker_dom.
DR   InterPro; IPR038255; PBS_linker_sf.
DR   InterPro; IPR016470; Phycobilisome.
DR   Pfam; PF01383; CpcD; 1.
DR   Pfam; PF00427; PBS_linker_poly; 1.
DR   PIRSF; PIRSF005898; Phycobilisome_CpeC/CpcI; 1.
DR   SMART; SM01094; CpcD; 1.
DR   PROSITE; PS51441; CPCD_LIKE; 1.
DR   PROSITE; PS51445; PBS_LINKER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antenna complex; Membrane; Photosynthesis; Phycobilisome;
KW   Reference proteome; Thylakoid.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..287
FT                   /note="Phycobilisome 32.1 kDa linker polypeptide,
FT                   phycocyanin-associated, rod"
FT                   /id="PRO_0000199221"
FT   DOMAIN          2..180
FT                   /note="PBS-linker"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT   DOMAIN          235..287
FT                   /note="CpcD-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT   HELIX           29..39
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   HELIX           56..63
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   HELIX           69..77
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   HELIX           92..103
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   HELIX           111..123
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   HELIX           126..135
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   HELIX           137..143
FT                   /evidence="ECO:0007829|PDB:2L8V"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:2L8V"
SQ   SEQUENCE   287 AA;  32124 MW;  9ED5E81ECB7FD68A CRC64;
     MAITAAASRL GTSAFSDAPP VELRANWSEE DLETVIRAVY RQVLGNDYVM ASERLVSAES
     LLRNGKITVR EFVRAVAKSE LYKEKFLYGN FQTRVIELNY KHLLGRAPYD ESEVIFHLDL
     YENEGFDADI DSYIDSPEYT NSFGDWVVPY YRGFNTQPGQ KTVGFNRIFR LYRGYANSDR
     AQAEGSMSRL ARDLATNRAN TVVPPSNSDT AFAYYTPSAD VPPRACLGGS FGESGRVYRI
     EVAGIRQPGY PGVRRSSTAF LVPYEQLSAK MQQLQRTGAR IISVNPA
 
 
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