PSBF_SPIOL
ID PSBF_SPIOL Reviewed; 39 AA.
AC P60128; P05171; P09198; Q6EYP5; Q95H58; Q9M3L1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hermann R.G., Alt J., Schiller B., Widger W.R., Cramer W.A.;
RT "Nucleotide sequence of the gene for apocytochrome b-559 on the spinach
RT plastid chromosome: implications for the structure of the membrane
RT protein.";
RL FEBS Lett. 176:239-244(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Graham S.W., Rai H.S., Ikegami K., Reeves P.A., Olmstead R.G.;
RT "Parsing out signal and noise for seed-plant phylogenetic inference.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [4]
RP PROTEIN SEQUENCE OF 2-9, AND BLOCKAGE OF N-TERMINUS.
RA Widger W.R., Cramer W.A., Hermodson M., Herrmann R.G.;
RT "Evidence for a hetero-oligomeric structure of the chloroplast cytochrome
RT b-559.";
RL FEBS Lett. 191:186-190(1985).
RN [5]
RP PROTEIN SEQUENCE OF 2-11, AND BLOCKAGE OF N-TERMINUS.
RX PubMed=2644131; DOI=10.1016/0014-5793(89)80482-x;
RA Ikeuchi M., Takio K., Inoue Y.;
RT "N-terminal sequencing of photosystem II low-molecular-mass proteins. 5 and
RT 4.1 kDa components of the O2-evolving core complex from higher plants.";
RL FEBS Lett. 242:263-269(1989).
RN [6]
RP RNA EDITING OF POSITION 25.
RX PubMed=8355656; DOI=10.1007/bf00277062;
RA Bock R., Hagemann R., Koessel H., Kudla J.;
RT "Tissue- and stage-specific modulation of RNA editing of the psbF and psbL
RT transcript from spinach plastids -- a new regulatory mechanism?";
RL Mol. Gen. Genet. 240:238-244(1993).
RN [7]
RP PROTEIN SEQUENCE OF 2-8, AND MASS SPECTROMETRY.
RX PubMed=9632665; DOI=10.1074/jbc.273.26.16122;
RA Zheleva D., Sharma J., Panico M., Morris H.R., Barber J.;
RT "Isolation and characterization of monomeric and dimeric CP47-reaction
RT center photosystem II complexes.";
RL J. Biol. Chem. 273:16122-16127(1998).
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 -!- PTM: The N-terminus is blocked.
CC -!- RNA EDITING: Modified_positions=26;
CC -!- MASS SPECTROMETRY: Mass=4409.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9632665};
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC Rule:MF_00643}.
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DR EMBL; M35673; AAA84629.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF528885; AAQ09328.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ400848; CAB88744.1; ALT_SEQ; Genomic_DNA.
DR PIR; S35262; S35262.
DR RefSeq; NP_054951.1; NC_002202.1.
DR PDB; 3JCU; EM; 3.20 A; F/f=1-39.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; P60128; -.
DR SMR; P60128; -.
DR DIP; DIP-62012N; -.
DR IntAct; P60128; 1.
DR STRING; 3562.P60128; -.
DR GeneID; 2715612; -.
DR KEGG; soe:2715612; -.
DR OrthoDB; 1637060at2759; -.
DR Proteomes; UP000054095; Chloroplast.
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; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Photosynthesis; Photosystem II;
KW Plastid; Reference proteome; RNA editing; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2644131,
FT ECO:0000269|PubMed:9632665, ECO:0000269|Ref.4"
FT CHAIN 2..39
FT /note="Cytochrome b559 subunit beta"
FT /id="PRO_0000200455"
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..35
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 39 AA; 4498 MW; 591251852D6E0A03 CRC64;
MTIDRTYPIF TVRWLAIHGL AVPTVFFLGS ISAMQFIQR
