ID   PSBF_ORYNI              Reviewed;          39 AA.
AC   Q6ENF7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
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   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SL10 {ECO:0000312|Proteomes:UP000006591};
RX   PubMed=15556301; DOI=10.1016/j.gene.2004.06.008;
RA   Masood M.S., Nishikawa T., Fukuoka S., Njenga P.K., Tsudzuki T.,
RA   Kadowaki K.;
RT   "The complete nucleotide sequence of wild rice (Oryza nivara) chloroplast
RT   genome: first genome wide comparative sequence analysis of wild and
RT   cultivated rice.";
RL   Gene 340:133-139(2004).
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   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00643}.
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DR   EMBL; AP006728; BAD26795.1; -; Genomic_DNA.
DR   RefSeq; YP_052766.1; NC_005973.1.
DR   AlphaFoldDB; Q6ENF7; -.
DR   SMR; Q6ENF7; -.
DR   GeneID; 2885952; -.
DR   Proteomes; UP000006591; 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:0009536; C:plastid; IC:Gramene.
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   3: Inferred from homology;
KW   Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Photosynthesis; Photosystem II; Plastid; Reference proteome; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..39
FT                   /note="Cytochrome b559 subunit beta"
FT                   /id="PRO_0000200433"
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"
SQ   SEQUENCE   39 AA;  4484 MW;  F61251852D6E1C6F CRC64;
     MTIDRTYPIF TVRWLAVHGL AVPTVFFLGS ISAMQFIQR