PYR1_SYNY3
ID PYR1_SYNY3 Reviewed; 291 AA.
AC P73203;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod 1;
GN Name=cpcC1; OrderedLocusNames=sll1580;
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 2-21.
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 [3]
RP 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 [4] {ECO:0007744|PDB:3PRU}
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 14-158.
RC STRAIN=PCC 6803 / Kazusa;
RA Kuzin A., Su M., Patel P., Xiao R., Ciccosanti C., Lee D., Everett J.K.,
RA Nair R., Acton T.B., Rost B., Montelione G.T., Tong L., Hunt J.F.;
RT "Northeast Structural Genomics Consortium Target SgR182A.";
RL Submitted (NOV-2010) to the PDB data bank.
CC -!- FUNCTION: Rod linker protein, connecting hexameric phycocyanin (PC,
CC made by cpcA and cpcB) rods in the phycobilisome (PBS). PC is the major
CC phycobiliprotein in PBS rods. Linker polypeptides determine the state
CC of aggregation and the location of the disk-shaped phycobiliprotein
CC units within the phycobilisome and modulate their spectroscopic
CC properties in order to mediate a directed and optimal energy transfer.
CC {ECO:0000269|PubMed:31015331}.
CC -!- SUBUNIT: Part of 2 PBS rod complexes, the conventional CpcG-PBS rod and
CC a photosystem I-specific CpcL-PBS rod, both of which include
CC ferredoxin--NADP reductase (petH). CpcG-PBS has on average 3 stacked
CC phycocyanin hexamers (PC, CpcA and CpcB). Linker CpcG connects the PC
CC stack to the thylakoid, the hexamers are linked by 1 copy of CpcC1, 1
CC copy of CpcC2 and the stack is terminated by a single copy of CpcD. The
CC CpcL-PBS has on average 5 stacked phycocyanin hexamers (PC, CpcA and
CC CpcB). Linker CpcL connects the PC stack to the thylakoid, the hexamers
CC are linked by 1 copy of CpcC1, 3 copies of CpcC2 and the stack is
CC terminated by a single copy of CpcD. {ECO:0000269|PubMed:31015331}.
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:0000269|PubMed:31015331}.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; BA000022; BAA17229.1; -; Genomic_DNA.
DR PIR; S75315; S75315.
DR PDB; 3PRU; X-ray; 2.68 A; A/B/C/D=14-158.
DR PDBsum; 3PRU; -.
DR AlphaFoldDB; P73203; -.
DR SMR; P73203; -.
DR IntAct; P73203; 2.
DR STRING; 1148.1652306; -.
DR PaxDb; P73203; -.
DR EnsemblBacteria; BAA17229; BAA17229; BAA17229.
DR KEGG; syn:sll1580; -.
DR eggNOG; COG0237; Bacteria.
DR InParanoid; P73203; -.
DR OMA; YNSFQTR; -.
DR PhylomeDB; P73203; -.
DR Proteomes; UP000001425; 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; Direct protein sequencing; Membrane;
KW Photosynthesis; Phycobilisome; Reference proteome; Thylakoid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298645"
FT CHAIN 2..291
FT /note="Phycobilisome 32.1 kDa linker polypeptide,
FT phycocyanin-associated, rod 1"
FT /id="PRO_0000199223"
FT DOMAIN 2..179
FT /note="PBS-linker"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 236..288
FT /note="CpcD-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:3PRU"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3PRU"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:3PRU"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:3PRU"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:3PRU"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3PRU"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:3PRU"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:3PRU"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:3PRU"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:3PRU"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3PRU"
SQ SEQUENCE 291 AA; 32521 MW; C6C1307D1910C687 CRC64;
MAITTAASRL GVAPYNESRP VELRPDFSLD DAKMVIRAVY RQVLGNDYIM DSERLKGAES
LLTNGSISVR EFVRTVAKSE LYKKKFLYNN FQTRVIELNY KHLLGRAPFS EDEVIFHLDL
YENQGFDADI DSYIDSVEYQ ENFGENIVPY YRFNNQVGDR TVGFTRMFRL YRGYANSDRS
QLERSSSRLA TELGQNTVSA IVGPSGSNAG WAYRPSRAGN TPAKALGGTV PFGQASKLFR
VEITAISAPG YPKVRRSNKA VIVPFEQLNQ TLQQINRLGG KVASITPASL S
