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Database: UniProt
Entry: A5GIA9_SYNPW
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ID   A5GIA9_SYNPW            Unreviewed;        45 AA.
AC   A5GIA9;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
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:CAK22674.1};
GN   OrderedLocusNames=SynWH7803_0248 {ECO:0000313|EMBL:CAK22674.1};
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK22674.1, ECO:0000313|Proteomes:UP000001566};
RN   [1] {ECO:0000313|Proteomes:UP000001566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00037211, ECO:0000256|HAMAP-Rule:MF_00643,
CC       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, peripheral proteins PsbO, CyanoQ (PsbQ), PsbU, PsbV and a
CC       large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000256|HAMAP-Rule:MF_00643}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00643, ECO:0000256|RuleBase:RU004529}; Single-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_00643,
CC       ECO:0000256|RuleBase:RU004529}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
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; CT971583; CAK22674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5GIA9; -.
DR   STRING; 32051.SynWH7803_0248; -.
DR   KEGG; syx:SynWH7803_0248; -.
DR   eggNOG; ENOG50332KX; Bacteria.
DR   HOGENOM; CLU_211753_1_0_3; -.
DR   OrthoDB; 532613at2; -.
DR   Proteomes; UP000001566; Chromosome.
DR   GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000001566};
KW   Thylakoid {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        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004529"
FT   DOMAIN          9..35
FT                   /note="Photosystem II cytochrome b559 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00283"
FT   BINDING         24
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   45 AA;  5065 MW;  FEA95792DB557D42 CRC64;
     MTQSPATSTP RNYPIFTVRW LAVHTLGVPT VFFLGALAAM QFIRR
//
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