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Database: UniProt
Entry: H8PFS8_9POAL
LinkDB: H8PFS8_9POAL
Original site: H8PFS8_9POAL 
ID   H8PFS8_9POAL            Unreviewed;        39 AA.
AC   H8PFS8;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Cytochrome b559 subunit beta {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
DE   AltName: Full=PSII reaction center subunit VI {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
GN   Name=psbF {ECO:0000256|HAMAP-Rule:MF_00643,
GN   ECO:0000313|EMBL:ADZ93718.1};
OS   Aratitiyopea lopezii.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:ADZ93718.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Xyridaceae; Aratitiyopea.
OX   NCBI_TaxID=196521 {ECO:0000313|EMBL:ADZ93718.1};
RN   [1] {ECO:0000313|EMBL:ADZ93718.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30368769; DOI=.1002/ajb2.1178;
RA   Givnish T.J., Zuluaga A., Spalink D., Soto Gomez M., Lam V.K.Y.,
RA   Saarela J.M., Sass C., Iles W.J.D., de Sousa D.J.L., Leebens-Mack J.,
RA   Chris Pires J., Zomlefer W.B., Gandolfo M.A., Davis J.I., Stevenson D.W.,
RA   dePamphilis C., Specht C.D., Graham S.W., Barrett C.F., Ane C.;
RT   "Monocot plastid phylogenomics, timeline, net rates of species
RT   diversification, the power of multi-gene analyses, and a functional model
RT   for the origin of monocots.";
RL   Am. J. Bot. 105:1888-1910(2018).
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:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00643};
CC       Note=With its partner (PsbE) binds heme. PSII binds additional
CC       chlorophylls, carotenoids and specific lipids. {ECO:0000256|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       Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving
CC       complex and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000256|HAMAP-Rule:MF_00643}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid,
CC       chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00643,
CC       ECO:0000256|RuleBase:RU004529}; Single-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
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DR   EMBL; EU832950; ADZ93718.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8PFS8; -.
DR   SMR; H8PFS8; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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   NCBIfam; TIGR01333; cyt_b559_beta; 1.
DR   Pfam; PF00283; Cytochrom_B559; 1.
DR   PIRSF; PIRSF000037; PsbF; 1.
DR   SUPFAM; SSF161045; Cytochrome b559 subunits; 1.
DR   PROSITE; PS00537; CYTOCHROME_B559; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|RuleBase:RU004529, ECO:0000313|EMBL:ADZ93718.1};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_00643};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00643};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00643};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW   Rule:MF_00643}; Plastid {ECO:0000313|EMBL:ADZ93718.1};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_00643};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00643}.
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004529"
FT   DOMAIN          1..29
FT                   /note="Photosystem II cytochrome b559 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00283"
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:0000256|HAMAP-Rule:MF_00643"
SQ   SEQUENCE   39 AA;  4424 MW;  F61251852D7E1D6F CRC64;
     MTIDRTYPIF TVRWLAVHGL AVPTVSFLGS ISAMQFIQR
//
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