ID   A0A097KPZ0_GEMMI        Unreviewed;        83 AA.
AC   A0A097KPZ0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   22-APR-2020, entry version 24.
DE   RecName: Full=Cytochrome b559 subunit alpha {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU000619};
DE   AltName: Full=PSII reaction center subunit V {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529};
GN   Name=psbE {ECO:0000256|HAMAP-Rule:MF_00642,
GN   ECO:0000313|EMBL:AIT95258.1};
OS   Geminella minor (Green alga) (Hormospora minor).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AIT95258.1}.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Geminella.
OX   NCBI_TaxID=163309 {ECO:0000313|EMBL:AIT95258.1};
RN   [1] {ECO:0000313|EMBL:AIT95258.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25270575; DOI=10.1186/s12862-014-0211-2;
RA   Lemieux C., Otis C., Turmel M.;
RT   "Chloroplast phylogenomic analysis resolves deep-level relationships within
RT   the green algal class Trebouxiophyceae.";
RL   BMC Evol. Biol. 14:211-211(2014).
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:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00642};
CC       Note=With its partner (PsbF) binds heme. PSII binds additional
CC       chlorophylls, carotenoids and specific lipids. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00642}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00642,
CC       ECO:0000256|RuleBase:RU004529}.
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00642, ECO:0000256|RuleBase:RU004529}.
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DR   EMBL; KM462883; AIT95258.1; -; Genomic_DNA.
DR   RefSeq; YP_009106452.1; NC_025544.1.
DR   GeneID; 22160777; -.
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   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|RuleBase:RU004529, ECO:0000313|EMBL:AIT95258.1};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_00642,
KW   ECO:0000256|RuleBase:RU004529};
KW   Heme {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00642,
KW   ECO:0000256|RuleBase:RU004529};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00642,
KW   ECO:0000256|RuleBase:RU004529};
KW   Photosystem II {ECO:0000256|HAMAP-Rule:MF_00642,
KW   ECO:0000256|RuleBase:RU004529}; Plastid {ECO:0000313|EMBL:AIT95258.1};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_00642};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00642,
KW   ECO:0000256|RuleBase:RU004529};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00642,
KW   ECO:0000256|RuleBase:RU004529};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00642, ECO:0000256|RuleBase:RU004529}.
FT   TRANSMEM        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004529"
FT   DOMAIN          6..34
FT                   /note="Cytochrom_B559"
FT                   /evidence="ECO:0000259|Pfam:PF00283"
FT   DOMAIN          42..79
FT                   /note="Cytochrom_B559a"
FT                   /evidence="ECO:0000259|Pfam:PF00284"
FT   METAL           23
FT                   /note="Iron (heme axial ligand); shared with beta subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00642"
SQ   SEQUENCE   83 AA;  9427 MW;  C71C0C971BE38907 CRC64;
     MSGSTGERPF SDILTSIRYW VIHSITIPSL FIAGWLFVST GLAYDVFGSP RPNEYFTEDR
     QEAPLITDRF NALEQVKQLS QVN
//