PSBF_GLOVI
ID PSBF_GLOVI Reviewed; 51 AA.
AC Q7NMA9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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}; OrderedLocusNames=gsr0857;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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: Cell inner 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; BA000045; BAC88798.1; -; Genomic_DNA.
DR RefSeq; NP_923803.1; NC_005125.1.
DR RefSeq; WP_011140859.1; NC_005125.1.
DR AlphaFoldDB; Q7NMA9; -.
DR SMR; Q7NMA9; -.
DR STRING; 251221.35211420; -.
DR EnsemblBacteria; BAC88798; BAC88798; BAC88798.
DR KEGG; gvi:gsr0857; -.
DR PATRIC; fig|251221.4.peg.874; -.
DR eggNOG; ENOG50332KX; Bacteria.
DR HOGENOM; CLU_211753_1_0_3; -.
DR InParanoid; Q7NMA9; -.
DR OrthoDB; 2060731at2; -.
DR PhylomeDB; Q7NMA9; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR GO; GO:0005886; C:plasma 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 Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Photosynthesis; Photosystem II;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..51
FT /note="Cytochrome b559 subunit beta"
FT /id="PRO_0000200468"
FT TRANSMEM 26..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00643"
FT BINDING 30
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 51 AA; 5576 MW; 422535A8E3D15418 CRC64;
MTTSSNRPTP GGPTQPVSYP VFTVRWLAVH ALTVPTIFFL GALAAMQFIQ R