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PSBE_CYAP4
ID   PSBE_CYAP4              Reviewed;          84 AA.
AC   B8HVD7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=Cyan7425_2228;
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece; unclassified Cyanothece.
OX   NCBI_TaxID=395961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7425 / ATCC 29141;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001344; ACL44589.1; -; Genomic_DNA.
DR   RefSeq; WP_012627666.1; NC_011884.1.
DR   AlphaFoldDB; B8HVD7; -.
DR   SMR; B8HVD7; -.
DR   STRING; 395961.Cyan7425_2228; -.
DR   EnsemblBacteria; ACL44589; ACL44589; Cyan7425_2228.
DR   KEGG; cyn:Cyan7425_2228; -.
DR   eggNOG; ENOG5032RR6; Bacteria.
DR   HOGENOM; CLU_194095_0_0_3; -.
DR   OMA; VRYWVIH; -.
DR   OrthoDB; 1863986at2; -.
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   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Photosynthesis;
KW   Photosystem II; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..84
FT                   /note="Cytochrome b559 subunit alpha"
FT                   /id="PRO_1000147429"
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"
SQ   SEQUENCE   84 AA;  9607 MW;  B925A9B6025739D7 CRC64;
     MAGTTGERPF SDIITSVRYW VIHSITIPAL FIAGWLFVST GLAYDVFGTP RPNEYYSQVR
     QELPIISDRL EGKQQINEFL KEVK
 
 
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