ID   PSBE_SYNR3              Reviewed;          83 AA.
AC   A5GQF4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=SynRCC307_0210;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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.
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}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00642}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00642}.
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00642}.
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DR   EMBL; CT978603; CAK27113.1; -; Genomic_DNA.
DR   RefSeq; WP_011934628.1; NC_009482.1.
DR   AlphaFoldDB; A5GQF4; -.
DR   SMR; A5GQF4; -.
DR   STRING; 316278.SynRCC307_0210; -.
DR   EnsemblBacteria; CAK27113; CAK27113; SynRCC307_0210.
DR   KEGG; syr:SynRCC307_0210; -.
DR   eggNOG; ENOG5032GCS; Bacteria.
DR   HOGENOM; CLU_194095_0_0_3; -.
DR   OMA; VRYWVIH; -.
DR   OrthoDB; 1863986at2; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW   Photosystem II; Reference proteome; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..83
FT                   /note="Cytochrome b559 subunit alpha"
FT                   /id="PRO_1000056933"
FT   TRANSMEM        22..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00642"
FT   BINDING         24
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"
SQ   SEQUENCE   83 AA;  9174 MW;  864E275656A84F1A CRC64;
     MAAGSTGERP FFEIITSIRY WVIHAVTLPA IFLAGFLFVS TGLAYDAFGT PRPDSYFQAA
     DVKAPVVSQR YEGKSQLDTR LKN