PSBE_SPIOL
ID PSBE_SPIOL Reviewed; 83 AA.
AC P69383; P09197;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cytochrome b559 subunit alpha {ECO:0000255|HAMAP-Rule:MF_00642};
DE AltName: Full=PSII reaction center subunit V {ECO:0000255|HAMAP-Rule:MF_00642};
GN Name=psbE {ECO:0000255|HAMAP-Rule:MF_00642};
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hermann R.G., Alt J., Schiller B., Widger W.R., Cramer W.A.;
RT "Nucleotide sequence of the gene for apocytochrome b-559 on the spinach
RT plastid chromosome: implications for the structure of the membrane
RT protein.";
RL FEBS Lett. 176:239-244(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-28.
RX PubMed=6706983; DOI=10.1016/s0021-9258(17)43178-4;
RA Widger W.R., Cramer W.A., Hermodson M., Meyer D., Gullifor M.;
RT "Purification and partial amino acid sequence of the chloroplast cytochrome
RT b-559.";
RL J. Biol. Chem. 259:3870-3876(1984).
RN [4]
RP PROTEIN SEQUENCE OF 2-15.
RX PubMed=2644131; DOI=10.1016/0014-5793(89)80482-x;
RA Ikeuchi M., Takio K., Inoue Y.;
RT "N-terminal sequencing of photosystem II low-molecular-mass proteins. 5 and
RT 4.1 kDa components of the O2-evolving core complex from higher plants.";
RL FEBS Lett. 242:263-269(1989).
RN [5]
RP PROTEIN SEQUENCE OF 2-7, AND MASS SPECTROMETRY.
RX PubMed=9632665; DOI=10.1074/jbc.273.26.16122;
RA Zheleva D., Sharma J., Panico M., Morris H.R., Barber J.;
RT "Isolation and characterization of monomeric and dimeric CP47-reaction
RT center photosystem II complexes.";
RL J. Biol. Chem. 273:16122-16127(1998).
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_00642}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00642};
CC Note=With its partner (PsbF) binds heme. PSII binds additional
CC chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC Rule:MF_00642};
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_00642}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00642}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00642}.
CC -!- MASS SPECTROMETRY: Mass=9255.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9632665};
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC Rule:MF_00642}.
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DR EMBL; M35673; AAA84628.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88745.1; -; Genomic_DNA.
DR PIR; S00418; S00418.
DR RefSeq; NP_054952.1; NC_002202.1.
DR PDB; 3JCU; EM; 3.20 A; E/e=1-83.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; P69383; -.
DR SMR; P69383; -.
DR DIP; DIP-62011N; -.
DR IntAct; P69383; 1.
DR STRING; 3562.P69383; -.
DR GeneID; 2715611; -.
DR KEGG; soe:2715611; -.
DR OrthoDB; 1506855at2759; -.
DR Proteomes; UP000054095; Chloroplast.
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 Gene3D; 1.20.5.860; -; 1.
DR HAMAP; MF_00642; PSII_PsbE; 1.
DR InterPro; IPR006217; PSII_cyt_b559_asu.
DR InterPro; IPR037025; PSII_cyt_b559_asu_sf.
DR InterPro; IPR006216; PSII_cyt_b559_CS.
DR InterPro; IPR013081; PSII_cyt_b559_N.
DR InterPro; IPR013082; PSII_cytb559_asu_lum.
DR Pfam; PF00283; Cytochrom_B559; 1.
DR Pfam; PF00284; Cytochrom_B559a; 1.
DR PIRSF; PIRSF000036; PsbE; 1.
DR TIGRFAMs; TIGR01332; cyt_b559_alpha; 1.
DR PROSITE; PS00537; CYTOCHROME_B559; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Photosynthesis; Photosystem II;
KW Plastid; Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2644131,
FT ECO:0000269|PubMed:6706983, ECO:0000269|PubMed:9632665"
FT CHAIN 2..83
FT /note="Cytochrome b559 subunit alpha"
FT /id="PRO_0000200339"
FT TRANSMEM 21..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00642"
FT BINDING 23
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with beta subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00642"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 17..39
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 83 AA; 9387 MW; F1E3918BCABACDDE CRC64;
MSGSTGERSF ADIITSIRYW VIHSITIPSL FIAGWLFVST GLAYDVFGSP RPNEYFTESR
QGIPLITGRF DSLEQLDEFS RSF
