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PSBE_PEA
ID   PSBE_PEA                Reviewed;          83 AA.
AC   P13554;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 113.
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   Pisum sativum (Garden pea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2766383; DOI=10.1007/bf00435508;
RA   Willey D.L., Gray J.C.;
RT   "Two small open reading frames are co-transcribed with the pea chloroplast
RT   genes for the polypeptides of cytochrome b-559.";
RL   Curr. Genet. 15:213-220(1989).
RN   [2]
RP   MASS SPECTROMETRY.
RX   PubMed=9407102; DOI=10.1074/jbc.272.52.33153;
RA   Sharma J., Panico M., Barber J., Morris H.R.;
RT   "Purification and determination of intact molecular mass by electrospray
RT   ionization mass spectrometry of the photosystem II reaction center
RT   subunits.";
RL   J. Biol. Chem. 272:33153-33157(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_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=9283.7; Mass_error=0.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9407102};
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00642}.
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DR   EMBL; X15767; CAA33772.1; -; Genomic_DNA.
DR   PIR; A48310; A48310.
DR   RefSeq; YP_003587551.1; NC_014057.1.
DR   PDB; 5XNL; EM; 2.70 A; E/e=1-83.
DR   PDB; 5XNM; EM; 3.20 A; E/e=1-83.
DR   PDB; 6YP7; EM; 3.80 A; E/e=8-82.
DR   PDBsum; 5XNL; -.
DR   PDBsum; 5XNM; -.
DR   PDBsum; 6YP7; -.
DR   AlphaFoldDB; P13554; -.
DR   SMR; P13554; -.
DR   EnsemblPlants; Psat0s6989g0160.1; Psat0s6989g0160.1.cds1; Psat0s6989g0160.
DR   GeneID; 9073099; -.
DR   Gramene; Psat0s6989g0160.1; Psat0s6989g0160.1.cds1; Psat0s6989g0160.
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; Electron transport; Heme; Iron; Membrane;
KW   Metal-binding; Photosynthesis; Photosystem II; Plastid; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9407102"
FT   CHAIN           2..83
FT                   /note="Cytochrome b559 subunit alpha"
FT                   /id="PRO_0000200329"
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..14
FT                   /evidence="ECO:0007829|PDB:5XNL"
FT   HELIX           17..39
FT                   /evidence="ECO:0007829|PDB:5XNL"
FT   HELIX           42..46
FT                   /evidence="ECO:0007829|PDB:5XNL"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:5XNM"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:5XNM"
FT   HELIX           72..81
FT                   /evidence="ECO:0007829|PDB:5XNL"
SQ   SEQUENCE   83 AA;  9415 MW;  F681641BCABAD2C1 CRC64;
     MSGSTGERSF ADIITSIRYW IIHSITIPSL FIAGWLFVST GLAYDVFGSP RPNEYFTETR
     QGIPLITGRF DSLEQLDEFS RSF
 
 
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