PHCB_SYNY3
ID PHCB_SYNY3 Reviewed; 172 AA.
AC Q54714; P73205;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=C-phycocyanin beta subunit;
GN Name=cpcB; OrderedLocusNames=sll1577;
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 [GENOMIC DNA].
RA Plank T., Anderson L.K.;
RT "Cloning and sequence analysis of the genes encoding CpcB and CpcA from
RT Synechocystis sp. PCC 6803.";
RL (er) Plant Gene Register PGR95-087(1995).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 1-16.
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 [4]
RP PROTEIN SEQUENCE OF 1-7, AND SUBUNIT.
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 [5]
RP INTERACTION WITH CPCC2, AND SUBUNIT.
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).
RN [6] {ECO:0007744|PDB:4F0T}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PHYCOCYANOBILIN
RP CHROMOPHORE, SUBUNIT, AND METHYLATION AT ASN-72.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=23201474; DOI=10.1016/j.bbabio.2012.11.006;
RA Marx A., Adir N.;
RT "Allophycocyanin and phycocyanin crystal structures reveal facets of
RT phycobilisome assembly.";
RL Biochim. Biophys. Acta 1827:311-318(2013).
CC -!- FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the
CC phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major
CC phycobiliprotein in the PBS rod.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain, which further
CC assembles into trimers. The trimers assemble into hexamers, although
CC these were not seen in the crystallographic studies (PubMed:23201474).
CC Part of 2 PBS rod complexes, the conventional CpcG-PBS rod and a
CC photosystem I-specific CpcL-PBS rod, both of which include ferredoxin--
CC NADP reductase (petH) (PubMed:31015331). Interacts with rod linker
CC CpcC2 via the latter's N-terminal PBS-linker domain (PubMed:21923764).
CC {ECO:0000269|PubMed:21923764, ECO:0000269|PubMed:23201474,
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=Part of the phycobilisome rod.
CC {ECO:0000269|PubMed:31015331}.
CC -!- PTM: Contains two covalently linked bilin chromophores.
CC {ECO:0000269|PubMed:23201474}.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR EMBL; U34930; AAA91032.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17232.1; -; Genomic_DNA.
DR PIR; S75318; S75318.
DR PDB; 4F0T; X-ray; 2.25 A; B=1-172.
DR PDBsum; 4F0T; -.
DR AlphaFoldDB; Q54714; -.
DR SMR; Q54714; -.
DR IntAct; Q54714; 5.
DR STRING; 1148.1652309; -.
DR PaxDb; Q54714; -.
DR PRIDE; Q54714; -.
DR EnsemblBacteria; BAA17232; BAA17232; BAA17232.
DR KEGG; syn:sll1577; -.
DR eggNOG; ENOG502Z7NE; Bacteria.
DR InParanoid; Q54714; -.
DR OMA; GITPGDC; -.
DR PhylomeDB; Q54714; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0030089; C:phycobilisome; IDA:UniProtKB.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.490.20; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012128; Phycobilisome_asu/bsu.
DR InterPro; IPR038719; Phycobilisome_asu/bsu_sf.
DR InterPro; IPR006247; Phycocyanin_b.
DR Pfam; PF00502; Phycobilisome; 1.
DR PIRSF; PIRSF000081; Phycocyanin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR TIGRFAMs; TIGR01339; phycocy_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Bile pigment; Chromophore;
KW Direct protein sequencing; Electron transport; Membrane; Methylation;
KW Photosynthesis; Phycobilisome; Reference proteome; Thylakoid; Transport.
FT CHAIN 1..172
FT /note="C-phycocyanin beta subunit"
FT /id="PRO_0000199161"
FT BINDING 82
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="1"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:23201474,
FT ECO:0007744|PDB:4F0T"
FT BINDING 153
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /ligand_label="2"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:23201474,
FT ECO:0007744|PDB:4F0T"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000269|PubMed:23201474,
FT ECO:0007744|PDB:4F0T"
FT CONFLICT 61
FT /note="A -> V (in Ref. 1; AAA91032)"
FT /evidence="ECO:0000305"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:4F0T"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:4F0T"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:4F0T"
FT HELIX 154..169
FT /evidence="ECO:0007829|PDB:4F0T"
SQ SEQUENCE 172 AA; 18126 MW; 82A0DE37AF20ADBA CRC64;
MFDVFTRVVS QADARGEYLS GSQLDALSAT VAEGNKRIDS VNRITGNASA IVSNAARALF
AEQPQLIQPG GNAYTSRRMA ACLRDMEIIL RYVTYATFTG DASVLEDRCL NGLRETYVAL
GVPGASVAAG VQKMKEAALD IVNDPNGITR GDCSAIVAEI AGYFDRAAAA VA
