PSBF_SYNS9
ID PSBF_SYNS9 Reviewed; 45 AA.
AC Q3B0C7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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};
GN OrderedLocusNames=Syncc9902_0226;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) 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: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.
CC Cyanobacterial PSII is composed of 1 copy each of membrane proteins
CC PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM,
CC PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins PsbO,
CC PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC {ECO:0000255|HAMAP-Rule:MF_00643}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00643}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00643}.
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC Rule:MF_00643}.
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DR EMBL; CP000097; ABB25201.1; -; Genomic_DNA.
DR RefSeq; WP_011359062.1; NC_007513.1.
DR AlphaFoldDB; Q3B0C7; -.
DR SMR; Q3B0C7; -.
DR STRING; 316279.Syncc9902_0226; -.
DR EnsemblBacteria; ABB25201; ABB25201; Syncc9902_0226.
DR KEGG; sye:Syncc9902_0226; -.
DR eggNOG; ENOG50332KX; Bacteria.
DR HOGENOM; CLU_211753_1_0_3; -.
DR OrthoDB; 2060731at2; -.
DR Proteomes; UP000002712; Chromosome.
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: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 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 Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW Photosystem II; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..45
FT /note="Cytochrome b559 subunit beta"
FT /id="PRO_0000233658"
FT TRANSMEM 20..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00643"
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:0000255|HAMAP-Rule:MF_00643"
SQ SEQUENCE 45 AA; 5107 MW; 8085719F178A4A60 CRC64;
MSQAPMATTP RNYPIFTVRW LALHTLGIPT VFFLGALAAM QFIRR
