PSBE_SYNY3
ID PSBE_SYNY3 Reviewed; 81 AA.
AC P09190;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
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}; OrderedLocusNames=ssr3451;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3130246; DOI=10.1002/j.1460-2075.1988.tb02816.x;
RA Pakrasi H.B., Williams J.G.K., Arntzen C.J.;
RT "Targeted mutagenesis of the psbE and psbF genes blocks photosynthetic
RT electron transport: evidence for a functional role of cytochrome b559 in
RT photosystem II.";
RL EMBO J. 7:325-332(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 2-12, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12069591; DOI=10.1021/bi026012+;
RA Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K.,
RA Pakrasi H.B.;
RT "Proteomic analysis of a highly active photosystem II preparation from the
RT cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel
RT polypeptides.";
RL Biochemistry 41:8004-8012(2002).
RN [4]
RP PROTEIN SEQUENCE OF 2-6.
RX PubMed=8536689; DOI=10.1111/j.1432-1033.1995.459_b.x;
RA Barbato R., Polverino De Laureto P., Rigoni F., De Martini E.,
RA Giacometti G.M.;
RT "Pigment-protein complexes from the photosynthetic membrane of the
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL Eur. J. Biochem. 234:459-465(1995).
RN [5]
RP MUTAGENESIS OF HIS-23.
RX PubMed=1904816; DOI=10.1002/j.1460-2075.1991.tb07684.x;
RA Pakrasi H.B., de Ciechi P., Whitmarsh J.;
RT "Site directed mutagenesis of the heme axial ligands of cytochrome b559
RT affects the stability of the photosystem II complex.";
RL EMBO J. 10:1619-1627(1991).
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 ECO:0000305|PubMed:1904816};
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.
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:12069591}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00642, ECO:0000269|PubMed:12069591}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00642}.
CC -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC Rule:MF_00642}.
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DR EMBL; M33897; AAA27299.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17092.1; -; Genomic_DNA.
DR PIR; S00338; CBYB55.
DR PDB; 6WJ6; EM; 2.58 A; E=1-81.
DR PDB; 7N8O; EM; 1.93 A; E/e=1-81.
DR PDB; 7RCV; EM; 2.01 A; E/e=1-81.
DR PDBsum; 6WJ6; -.
DR PDBsum; 7N8O; -.
DR PDBsum; 7RCV; -.
DR AlphaFoldDB; P09190; -.
DR SMR; P09190; -.
DR IntAct; P09190; 5.
DR STRING; 1148.1652168; -.
DR PaxDb; P09190; -.
DR EnsemblBacteria; BAA17092; BAA17092; BAA17092.
DR KEGG; syn:ssr3451; -.
DR eggNOG; ENOG5032RR6; Bacteria.
DR InParanoid; P09190; -.
DR OMA; VRYWVIH; -.
DR Proteomes; UP000001425; Chromosome.
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:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB.
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;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12069591,
FT ECO:0000269|PubMed:8536689"
FT CHAIN 2..81
FT /note="Cytochrome b559 subunit alpha"
FT /id="PRO_0000200347"
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 ECO:0000305|PubMed:1904816"
FT MUTAGEN 23
FT /note="H->L: Complete loss of PSII activity, decreased
FT accumulation of PSII subunits, altered mobility of the PsbE
FT subunit."
FT /evidence="ECO:0000269|PubMed:1904816"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 17..39
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:7N8O"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:7N8O"
SQ SEQUENCE 81 AA; 9449 MW; 36006882C691CC99 CRC64;
MSGTTGERPF SDIVTSIRYW VIHSITIPML FIAGWLFVST GLAYDAFGTP RPDEYFTQTR
QELPILQERY DINQEIQEFN Q
