PSBE_THEVL
ID PSBE_THEVL Reviewed; 84 AA.
AC P12238; Q8GI50;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
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 Thermostichus vulcanus (Synechococcus vulcanus).
OC Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX NCBI_TaxID=32053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8 AND 74-84,
RP COMPOSITION OF PHOTOSYSTEM II, AND SUBUNIT.
RX PubMed=12461137; DOI=10.1093/pcp/pcf168;
RA Kashino Y., Koike H., Yoshio M., Egashira H., Ikeuchi M., Pakrasi H.B.,
RA Satoh K.;
RT "Low-molecular-mass polypeptide components of a photosystem II preparation
RT from the thermophilic cyanobacterium Thermosynechococcus vulcanus.";
RL Plant Cell Physiol. 43:1366-1373(2002).
RN [2]
RP PROTEIN SEQUENCE OF 2-34.
RX DOI=10.1016/0014-5793(89)81446-2;
RA Ikeuchi M., Koike H., Inoue Y.;
RT "Identification of psbI and psbL gene products in cyanobacterial
RT photosystem II reaction center preparation.";
RL FEBS Lett. 251:155-160(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 2-84 IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12518057; DOI=10.1073/pnas.0135651100;
RA Kamiya N., Shen J.-R.;
RT "Crystal structure of oxygen-evolving photosystem II from
RT Thermosynechococcus vulcanus at 3.7-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:98-103(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 3-84 IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19433803; DOI=10.1073/pnas.0812797106;
RA Kawakami K., Umena Y., Kamiya N., Shen J.R.;
RT "Location of chloride and its possible functions in oxygen-evolving
RT photosystem II revealed by X-ray crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8567-8572(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-84 IN COMPLEX WITH HEME IN
RP PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21499260; DOI=10.1038/nature09913;
RA Umena Y., Kawakami K., Shen J.R., Kamiya N.;
RT "Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9
RT A.";
RL Nature 473:55-60(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4-83 IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23426624; DOI=10.1073/pnas.1219922110;
RA Koua F.H., Umena Y., Kawakami K., Shen J.R.;
RT "Structure of Sr-substituted photosystem II at 2.1 A resolution and its
RT implications in the mechanism of water oxidation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3889-3894(2013).
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, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:23426624}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00642,
CC ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624};
CC Note=With its partner (PsbF) binds heme. PSII binds additional
CC chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
CC Rule:MF_00642, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624};
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_00642, ECO:0000269|PubMed:12461137,
CC ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00642, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}.
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC Rule:MF_00642}.
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DR EMBL; AB086860; BAC53634.1; -; Genomic_DNA.
DR PIR; S05030; S05030.
DR PDB; 1IZL; X-ray; 3.70 A; E/P=2-84.
DR PDB; 3A0B; X-ray; 3.70 A; E/e=3-84.
DR PDB; 3A0H; X-ray; 4.00 A; E/e=3-84.
DR PDB; 3WU2; X-ray; 1.90 A; E/e=2-84.
DR PDB; 4IL6; X-ray; 2.10 A; E/e=4-83.
DR PDB; 4UB6; X-ray; 1.95 A; E/e=1-84.
DR PDB; 4UB8; X-ray; 1.95 A; E/e=1-84.
DR PDB; 5B5E; X-ray; 1.87 A; E/e=2-84.
DR PDB; 5B66; X-ray; 1.85 A; E/e=2-84.
DR PDB; 5GTH; X-ray; 2.50 A; E/e=1-84.
DR PDB; 5GTI; X-ray; 2.50 A; E/e=1-84.
DR PDB; 5V2C; X-ray; 1.90 A; E/e=2-84.
DR PDB; 5WS5; X-ray; 2.35 A; E/e=1-84.
DR PDB; 5WS6; X-ray; 2.35 A; E/e=1-84.
DR PDB; 6JLJ; X-ray; 2.15 A; E/e=1-84.
DR PDB; 6JLK; X-ray; 2.15 A; E/e=1-84.
DR PDB; 6JLL; X-ray; 2.15 A; E/e=1-84.
DR PDB; 6JLM; X-ray; 2.35 A; E/e=1-84.
DR PDB; 6JLN; X-ray; 2.40 A; E/e=1-84.
DR PDB; 6JLO; X-ray; 2.40 A; E/e=1-84.
DR PDB; 6JLP; X-ray; 2.50 A; E/e=1-84.
DR PDB; 7CJI; X-ray; 2.35 A; E/e=1-84.
DR PDB; 7CJJ; X-ray; 2.40 A; E/e=1-84.
DR PDB; 7COU; X-ray; 2.25 A; E/e=1-84.
DR PDB; 7CZL; EM; 3.78 A; E/e=20-84.
DR PDB; 7D1T; EM; 1.95 A; E/e=4-84.
DR PDB; 7D1U; EM; 2.08 A; E/e=4-84.
DR PDB; 7DXA; EM; 3.14 A; e=1-84.
DR PDB; 7DXH; EM; 3.14 A; e=1-84.
DR PDB; 7EDA; EM; 2.78 A; E=1-84.
DR PDBsum; 1IZL; -.
DR PDBsum; 3A0B; -.
DR PDBsum; 3A0H; -.
DR PDBsum; 3WU2; -.
DR PDBsum; 4IL6; -.
DR PDBsum; 4UB6; -.
DR PDBsum; 4UB8; -.
DR PDBsum; 5B5E; -.
DR PDBsum; 5B66; -.
DR PDBsum; 5GTH; -.
DR PDBsum; 5GTI; -.
DR PDBsum; 5V2C; -.
DR PDBsum; 5WS5; -.
DR PDBsum; 5WS6; -.
DR PDBsum; 6JLJ; -.
DR PDBsum; 6JLK; -.
DR PDBsum; 6JLL; -.
DR PDBsum; 6JLM; -.
DR PDBsum; 6JLN; -.
DR PDBsum; 6JLO; -.
DR PDBsum; 6JLP; -.
DR PDBsum; 7CJI; -.
DR PDBsum; 7CJJ; -.
DR PDBsum; 7COU; -.
DR PDBsum; 7CZL; -.
DR PDBsum; 7D1T; -.
DR PDBsum; 7D1U; -.
DR PDBsum; 7DXA; -.
DR PDBsum; 7DXH; -.
DR PDBsum; 7EDA; -.
DR AlphaFoldDB; P12238; -.
DR SMR; P12238; -.
DR DIP; DIP-48862N; -.
DR IntAct; P12238; 1.
DR EvolutionaryTrace; P12238; -.
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:0031676; C:plasma membrane-derived thylakoid 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 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; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Photosynthesis; Photosystem II; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12461137, ECO:0000269|Ref.2"
FT CHAIN 2..84
FT /note="Cytochrome b559 subunit alpha"
FT /id="PRO_0000200346"
FT TOPO_DOM 2..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 21..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00642,
FT ECO:0000269|PubMed:21499260"
FT TOPO_DOM 36..84
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00642,
FT ECO:0000269|PubMed:21499260"
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 ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT ECO:0000303|PubMed:19433803"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 17..39
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5B5E"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:5B66"
SQ SEQUENCE 84 AA; 9573 MW; 19C7A074624D937F CRC64;
MAGTTGERPF SDIITSVRYW VIHSITIPAL FIAGWLFVST GLAYDVFGTP RPDSYYAQEQ
RSIPLVTDRF EAKQQVETFL EQLK
