PSBF_PEA
ID PSBF_PEA Reviewed; 39 AA.
AC P62096; P05172; Q7HIU4;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cytochrome b559 subunit beta {ECO:0000255|HAMAP-Rule:MF_00643};
DE AltName: Full=PSII reaction center subunit VI {ECO:0000255|HAMAP-Rule:MF_00643};
GN Name=psbF {ECO:0000255|HAMAP-Rule:MF_00643};
OS Pisum sativum (Garden pea).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2766383; DOI=10.1007/bf00435508;
RA Willey D.L., Gray J.C.;
RT "Two small open reading frames are co-transcribed with the pea chloroplast
RT genes for the polypeptides of cytochrome b-559.";
RL Curr. Genet. 15:213-220(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Graham S.W., Reeves P.A., Burns A., Olmstead R.G.;
RT "Long branches in the seed plants and the root of the angiosperms.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MASS SPECTROMETRY.
RX PubMed=9407102; DOI=10.1074/jbc.272.52.33153;
RA Sharma J., Panico M., Barber J., Morris H.R.;
RT "Purification and determination of intact molecular mass by electrospray
RT ionization mass spectrometry of the photosystem II reaction center
RT subunits.";
RL J. Biol. Chem. 272:33153-33157(1997).
CC -!- FUNCTION: This b-type cytochrome is tightly associated with the
CC reaction center of photosystem II (PSII). PSII is a light-driven
CC water:plastoquinone oxidoreductase that uses light energy to abstract
CC electrons from H(2)O, generating O(2) and a proton gradient
CC subsequently used for ATP formation. It consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation.
CC {ECO:0000255|HAMAP-Rule:MF_00643}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00643};
CC Note=With its partner (PsbE) binds heme. PSII binds additional
CC chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC Rule:MF_00643};
CC -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit. PSII is
CC composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD,
CC PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ,
CC Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex
CC and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000255|HAMAP-Rule:MF_00643}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00643}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00643}.
CC -!- MASS SPECTROMETRY: Mass=4394.8; Mass_error=0.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9407102};
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC Rule:MF_00643}.
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DR EMBL; X15767; CAA33773.1; -; Genomic_DNA.
DR EMBL; AY007482; AAG27011.1; -; Genomic_DNA.
DR PIR; B48310; B48310.
DR RefSeq; YP_003587552.1; NC_014057.1.
DR PDB; 5XNL; EM; 2.70 A; F/f=1-39.
DR PDB; 5XNM; EM; 3.20 A; F/f=1-39.
DR PDB; 6YP7; EM; 3.80 A; F/f=10-39.
DR PDBsum; 5XNL; -.
DR PDBsum; 5XNM; -.
DR PDBsum; 6YP7; -.
DR AlphaFoldDB; P62096; -.
DR SMR; P62096; -.
DR GeneID; 9073100; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro.
DR HAMAP; MF_00643; PSII_PsbF; 1.
DR InterPro; IPR006241; PSII_cyt_b559_bsu.
DR InterPro; IPR006216; PSII_cyt_b559_CS.
DR InterPro; IPR013081; PSII_cyt_b559_N.
DR PANTHER; PTHR33391:SF14; PTHR33391:SF14; 1.
DR Pfam; PF00283; Cytochrom_B559; 1.
DR PIRSF; PIRSF000037; PsbF; 1.
DR TIGRFAMs; TIGR01333; cyt_b559_beta; 1.
DR PROSITE; PS00537; CYTOCHROME_B559; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Photosynthesis; Photosystem II; Plastid; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..39
FT /note="Cytochrome b559 subunit beta"
FT /id="PRO_0000200436"
FT TRANSMEM 14..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00643"
FT BINDING 18
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with alpha subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00643"
FT HELIX 12..34
FT /evidence="ECO:0007829|PDB:5XNL"
SQ SEQUENCE 39 AA; 4424 MW; F61251852D7E1D6F CRC64;
MTIDRTYPIF TVRWLAVHGL AVPTVSFLGS ISAMQFIQR
