PYR2_SYNY3
ID PYR2_SYNY3 Reviewed; 273 AA.
AC P73204;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod 2;
DE AltName: Full=LR30 {ECO:0000303|PubMed:21923764};
GN Name=cpcC2; OrderedLocusNames=sll1579;
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 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] {ECO:0007744|PDB:3NPH}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-157, INTERACTION WITH
RP PHYCOCYANIN BETA SUBUNIT, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-26;
RP GLU-29; GLU-31; ASP-33; ARG-41; ASP-47; HIS-48; ARG-54; GLU-80 AND GLU-141.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=21923764; DOI=10.1111/j.1365-2958.2011.07844.x;
RA Gao X., Zhang N., Wei T.D., Su H.N., Xie B.B., Dong C.C., Zhang X.Y.,
RA Chen X.L., Zhou B.C., Wang Z.X., Wu J.W., Zhang Y.Z.;
RT "Crystal structure of the N-terminal domain of linker L(R) and the assembly
RT of cyanobacterial phycobilisome rods.";
RL Mol. Microbiol. 82:698-705(2011).
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 -!- 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 (PubMed:31015331). Interacts with
CC the C-phycocyanin (PC) beta subunit (cpcB), it may fit into the center
CC of the PC hexamer (PubMed:21923764). {ECO:0000269|PubMed:21923764,
CC 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 ECO:0000305|PubMed:21923764}.
CC -!- DOMAIN: The N-terminal PBS-linker domain (residues 19-157 in this
CC experiment) interacts with the C-phycocyanin beta subunit (cpcB).
CC {ECO:0000269|PubMed:21923764}.
CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU00775}.
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DR EMBL; BA000022; BAA17230.1; -; Genomic_DNA.
DR PIR; S75316; S75316.
DR PDB; 3NPH; X-ray; 1.85 A; B=19-157.
DR PDBsum; 3NPH; -.
DR AlphaFoldDB; P73204; -.
DR SMR; P73204; -.
DR IntAct; P73204; 2.
DR STRING; 1148.1652307; -.
DR PaxDb; P73204; -.
DR EnsemblBacteria; BAA17230; BAA17230; BAA17230.
DR KEGG; syn:sll1579; -.
DR eggNOG; COG0237; Bacteria.
DR InParanoid; P73204; -.
DR OMA; RNQKTVG; -.
DR PhylomeDB; P73204; -.
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; Membrane; Photosynthesis; Phycobilisome;
KW Reference proteome; Thylakoid.
FT CHAIN 1..273
FT /note="Phycobilisome 32.1 kDa linker polypeptide,
FT phycocyanin-associated, rod 2"
FT /id="PRO_0000199224"
FT DOMAIN 1..180
FT /note="PBS-linker"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00775"
FT DOMAIN 220..273
FT /note="CpcD-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT MUTAGEN 26
FT /note="R->E: Significantly decreases interaction of PBS-
FT linker domain with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 29
FT /note="E->R: Significantly decreases interaction of PBS-
FT linker domain with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 31
FT /note="E->R: Significantly decreases interaction of PBS-
FT linker domain with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 33
FT /note="D->R: Significantly decreases interaction of PBS-
FT linker domain with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 41
FT /note="R->E: Significantly decreases interaction of PBS-
FT linker domain with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 47
FT /note="D->R: Significantly decreases interaction of PBS-
FT linker domain with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 48
FT /note="H->Y: Significantly decreases interaction of PBS-
FT linker domain with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 54
FT /note="R->E: Significantly decreases interaction of PBS-
FT linker domain with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 80
FT /note="E->R: No change in interaction of PBS-linker domain
FT with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT MUTAGEN 141
FT /note="E->R: No change in interaction of PBS-linker domain
FT with phycocyanin beta subunit (cpcB)."
FT /evidence="ECO:0000269|PubMed:21923764"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3NPH"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:3NPH"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3NPH"
FT HELIX 56..63
FT /evidence="ECO:0007829|PDB:3NPH"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:3NPH"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:3NPH"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3NPH"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:3NPH"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3NPH"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:3NPH"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:3NPH"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:3NPH"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3NPH"
SQ SEQUENCE 273 AA; 30797 MW; 6E77BAB02A8BD354 CRC64;
MTSLVSAQRL GIVAVDEAIP LELRSRSTEE EVDAVILAVY RQVLGNDHLM SQERLTSAES
LLRGREISVR DFVRAVALSE VYRQKFFHSN PQNRFIELNY KHLLGRAPYD QSEIAFHTDL
YHQGGYEAEI NSYIDSVEYT ENFGDWVVPY FRGFATQRNQ KTVGFSRSFQ VYRGYATSDR
SQGNGSRSRL TRELARNTAS PVYAGSTAES LRGTSAGSRN QMYRLQVIQG AAPGRGTRVR
RGKAEYLVSY DNLSAKLQQI NRQGDTVTMI SLA
