PHCB_POLUR
ID PHCB_POLUR Reviewed; 172 AA.
AC P59859;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=R-phycocyanin beta chain;
GN Name=rpcB;
OS Polysiphonia urceolata (Red alga) (Conferva urceolata).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC Rhodomelaceae; Polysiphonioideae; Polysiphonia.
OX NCBI_TaxID=65404;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH RPCA; PHYCOCYANOBILIN
RP AND PHYCOERYTHROBILIN, FUNCTION, AND SUBUNIT.
RX PubMed=11463658; DOI=10.1016/s0006-3495(01)75774-8;
RA Jiang T., Zhang J.P., Chang W.R., Liang D.C.;
RT "Crystal structure of R-phycocyanin and possible energy transfer pathways
RT in the phycobilisome.";
RL Biophys. J. 81:1171-1179(2001).
CC -!- FUNCTION: Light-harvesting photosynthetic tetrapyrrole chromophore-
CC protein from the phycobiliprotein complex (phycobilisome, PBS).
CC Phycocyanin is the major phycobiliprotein in the PBS rod.
CC {ECO:0000269|PubMed:11463658}.
CC -!- SUBUNIT: Heterododecamer of 6 alpha and 6 beta chains. The basic
CC functional unit of phycobiliproteins is a ring-shaped hexamer formed
CC from two back-to-back trimers contacting via the alpha chain subunits.
CC The trimers are composed of alpha/beta subunit heterodimers arranged
CC around a three-fold axis of symmetry. The phycoerythrins also contain a
CC gamma subunit which is located in the center of the hexamer.
CC {ECO:0000269|PubMed:11463658}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC Peripheral membrane protein; Stromal side. Note=Part of the
CC phycobilisome rod.
CC -!- PTM: Contains one covalently linked phycocyanobilin chromophore and one
CC covalently linked phycoerythrobilin chromophore.
CC {ECO:0000269|PubMed:11463658}.
CC -!- MISCELLANEOUS: The light-harvesting antenna system in red algae and
CC cyanobacteria is formed of phycobilisomes. These are composed of the
CC phycobiliproteins phycoerythrin (CPE), phycocyanin (CPC) and
CC allophycocyanin (APC). Cyanobacteria also contain phycoerythrocyanin
CC (PCC). The phycobiliproteins all share the same subunit composition and
CC organization with variations in the covalently bound open-chain
CC tetrapyrrole chromophores. The phycobiliprotein complexes are arranged
CC sequentially in antenna complexes linked by linker proteins with CPE at
CC the periphery, CPC in the middle and APC at the core feeding to the
CC photosynthetic reaction center.
CC -!- SIMILARITY: Belongs to the phycobiliprotein family. {ECO:0000305}.
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DR PDB; 1F99; X-ray; 2.40 A; B/L/N=1-172.
DR PDBsum; 1F99; -.
DR AlphaFoldDB; P59859; -.
DR SMR; P59859; -.
DR EvolutionaryTrace; P59859; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
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; Chloroplast; Chromophore;
KW Electron transport; Membrane; Methylation; Photosynthesis; Phycobilisome;
KW Plastid; Thylakoid; Transport.
FT CHAIN 1..172
FT /note="R-phycocyanin beta chain"
FT /id="PRO_0000199162"
FT BINDING 35
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /evidence="ECO:0000269|PubMed:11463658"
FT BINDING 39
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /evidence="ECO:0000269|PubMed:11463658"
FT BINDING 72
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /evidence="ECO:0000269|PubMed:11463658"
FT BINDING 82
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:11463658"
FT BINDING 84..85
FT /ligand="(2R,3E)-phycocyanobilin"
FT /ligand_id="ChEBI:CHEBI:85275"
FT BINDING 149..151
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT BINDING 153
FT /ligand="(2R,3E)-phycoerythrobilin"
FT /ligand_id="ChEBI:CHEBI:85276"
FT /note="covalent, via 1 link"
FT /evidence="ECO:0000269|PubMed:11463658"
FT MOD_RES 72
FT /note="N4-methylasparagine"
FT /evidence="ECO:0000250"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1F99"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:1F99"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1F99"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:1F99"
SQ SEQUENCE 172 AA; 18001 MW; 6737DF9F0E0D52AF CRC64;
MLDAFAKVVA QADARGEFLS NTQIDALLAI VSEGNKRLDV VNKITNNASA IVTNAARALF
AEQPQLISPG GNAYTSRRMA ACLRDMEIVL RYVSYAMIAG DASVLDDRCL NGLRETYQAL
GTPGASVAVA IQKMKDAALA LVNDTTGTPA GDCASLVAEI ATYFDRAAAA VA
