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Database: UniProt
Entry: H6CSL6_ORYRU
LinkDB: H6CSL6_ORYRU
Original site: H6CSL6_ORYRU 
ID   H6CSL6_ORYRU            Unreviewed;        39 AA.
AC   H6CSL6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Cytochrome b559 subunit beta {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
DE   AltName: Full=PSII reaction center subunit VI {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
GN   Name=psbF {ECO:0000256|HAMAP-Rule:MF_00643,
GN   ECO:0000313|EMBL:AEI53107.1};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AEI53107.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EMBL:AEI53107.1, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|EMBL:AEI53107.1, ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W1943 {ECO:0000313|Proteomes:UP000008022};
RX   PubMed=22408737; DOI=10.1002/ece3.66;
RA   Waters D.L.E., Nock C.J., Rice N., Ishikawa R., Henry R.J.;
RT   "Chloroplast genome sequence confirms distinctness of Australian and Asian
RT   wild rice.";
RL   Ecol. Evol. 2:211-217(2012).
RN   [2] {ECO:0000313|EMBL:AGY93212.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Pilkington S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AGZ19230.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Lin Z., Fan L.;
RT   "The chloroplast genome of Chinese wild rice (Dongxiang).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AGY48963.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25329378;
RA   Brozynska M., Furtado A., Henry R.J.;
RT   "Direct chloroplast sequencing: comparison of sequencing platforms and
RT   analysis tools for whole chloroplast barcoding.";
RL   PLoS ONE 9:E110387-E110387(2014).
RN   [5] {ECO:0000313|EMBL:AJC09655.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Chen X.-L., Norrbom A., Zhu C.-D.;
RT   "A systematic study of Ichneumonosoma Meijere, Pelmatops Enderlein,
RT   Pseudopelmatops Shiraki and Soita Walker (Diptera: Tephritidae).";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:QTW91022.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Or135 {ECO:0000313|EMBL:QTW91022.1}, and Or136
RC   {ECO:0000313|EMBL:QTW91108.1};
RA   Li T.-Z.;
RL   Submitted (MAR-2021) 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:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00643};
CC       Note=With its partner (PsbE) binds heme. PSII binds additional
CC       chlorophylls, carotenoids and specific lipids. {ECO:0000256|HAMAP-
CC       Rule:MF_00643};
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       Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-evolving
CC       complex and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000256|HAMAP-Rule:MF_00643}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid,
CC       chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00643,
CC       ECO:0000256|RuleBase:RU004529}; Single-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
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DR   EMBL; JN005832; AEI53107.1; -; Genomic_DNA.
DR   EMBL; JN005833; AEI53184.1; -; Genomic_DNA.
DR   EMBL; KF428978; AGY48963.1; -; Genomic_DNA.
DR   EMBL; KF359902; AGY93212.1; -; Genomic_DNA.
DR   EMBL; KF562709; AGZ19230.1; -; Genomic_DNA.
DR   EMBL; KM103372; AJC09655.1; -; Genomic_DNA.
DR   EMBL; MW711321; QTW91022.1; -; Genomic_DNA.
DR   EMBL; MW711322; QTW91108.1; -; Genomic_DNA.
DR   RefSeq; YP_006280775.1; NC_017835.1.
DR   AlphaFoldDB; H6CSL6; -.
DR   SMR; H6CSL6; -.
DR   STRING; 4529.H6CSL6; -.
DR   GeneID; 12486641; -.
DR   Proteomes; UP000008022; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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   HAMAP; MF_00643; PSII_PsbF; 1.
DR   InterPro; IPR006241; PSII_cyt_b559_bsu.
DR   InterPro; IPR006216; PSII_cyt_b559_CS.
DR   InterPro; IPR013081; PSII_cyt_b559_N.
DR   NCBIfam; TIGR01333; cyt_b559_beta; 1.
DR   Pfam; PF00283; Cytochrom_B559; 1.
DR   PIRSF; PIRSF000037; PsbF; 1.
DR   SUPFAM; SSF161045; Cytochrome b559 subunits; 1.
DR   PROSITE; PS00537; CYTOCHROME_B559; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|RuleBase:RU004529, ECO:0000313|EMBL:AEI53107.1};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_00643};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00643};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00643};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Photosystem II {ECO:0000256|ARBA:ARBA00023276, ECO:0000256|HAMAP-
KW   Rule:MF_00643}; Plastid {ECO:0000313|EMBL:AEI53107.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_00643};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00643};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00643}.
FT   TRANSMEM        15..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004529"
FT   DOMAIN          1..29
FT                   /note="Photosystem II cytochrome b559 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00283"
FT   BINDING         18
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_note="ligand shared with alpha subunit"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00643"
SQ   SEQUENCE   39 AA;  4484 MW;  F61251852D6E1C6F CRC64;
     MTIDRTYPIF TVRWLAVHGL AVPTVFFLGS ISAMQFIQR
//
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