PSBF_CUSPE
ID PSBF_CUSPE Reviewed; 39 AA.
AC Q7H825;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Cuscuta pentagona (Five-angled dodder).
OG Plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Grammica; Cuscuta sect. Cleistogrammica.
OX NCBI_TaxID=112407;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND23320510;
RA Stefanovic S., Krueger L., Olmstead R.G.;
RT "Monophyly of the Convolvulaceae and circumscription of their major
RT lineages based on DNA sequences of multiple chloroplast loci.";
RL Am. J. Bot. 89:1510-1522(2002).
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 membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00643}.
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC Rule:MF_00643}.
CC -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC some thylakoids, although the photosynthetic activity does not exceed
CC the light compensation point. {ECO:0000305}.
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DR EMBL; AY100952; AAM53419.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7H825; -.
DR SMR; Q7H825; -.
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:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule.
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; Plastid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..39
FT /note="Cytochrome b559 subunit beta"
FT /id="PRO_0000200382"
FT TRANSMEM 14..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00643"
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:0000255|HAMAP-Rule:MF_00643"
SQ SEQUENCE 39 AA; 4498 MW; F6043D552D6E1C6F CRC64;
MTIDRTYPIF TVRWLAVHGL AIPTVFFLGS ISAMQFIQR