PSBF_CHLVU
ID PSBF_CHLVU Reviewed; 41 AA.
AC P56310;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Chlorella vulgaris (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3077;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM C-27 / Tamiya;
RX PubMed=9159184; DOI=10.1073/pnas.94.11.5967;
RA Wakasugi T., Nagai T., Kapoor M., Sugita M., Ito M., Ito S., Tsudzuki J.,
RA Nakashima K., Tsudzuki T., Suzuki Y., Hamada A., Ohta T., Inamura A.,
RA Yoshinaga K., Sugiura M.;
RT "Complete nucleotide sequence of the chloroplast genome from the green alga
RT Chlorella vulgaris: the existence of genes possibly involved in chloroplast
RT division.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5967-5972(1997).
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; AB001684; BAA57902.1; -; Genomic_DNA.
DR PIR; T07255; T07255.
DR RefSeq; NP_045827.1; NC_001865.1.
DR AlphaFoldDB; P56310; -.
DR GeneID; 809099; -.
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: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; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..41
FT /note="Cytochrome b559 subunit beta"
FT /id="PRO_0000200374"
FT TRANSMEM 16..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00643"
FT BINDING 20
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 41 AA; 4718 MW; 0537FC973058E8D6 CRC64;
MTARKSYTYP IFTVRWLAVH ALAVPTVFFL GAITAMQFIQ R