(data stored in SCRATCH zone)

SWISSPROT: A5GQF3_SYNR3

ID   A5GQF3_SYNR3            Unreviewed;        45 AA.
AC   A5GQF3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 69.
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:CAK27112.1};
GN   OrderedLocusNames=SynRCC307_0209 {ECO:0000313|EMBL:CAK27112.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27112.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
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
CC       abstract electrons from H(2)O, generating O(2) and a proton
CC       gradient subsequently used for ATP formation. It consists of a
CC       core antenna complex that captures photons, and an electron
CC       transfer chain that converts photonic excitation into a charge
CC       separation. {ECO:0000256|HAMAP-Rule:MF_00643,
CC       ECO:0000256|RuleBase:RU004529}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|HAMAP-
CC         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.
CC       Cyanobacterial PSII is composed of 1 copy each of membrane
CC       proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ,
CC       PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3
CC       peripheral proteins PsbO, PsbU, PsbV and a large number of
CC       cofactors. It forms dimeric complexes. {ECO:0000256|HAMAP-
CC       Rule:MF_00643}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00643,
CC       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; CT978603; CAK27112.1; -; Genomic_DNA.
DR   STRING; 316278.SynRCC307_0209; -.
DR   EnsemblBacteria; CAK27112; CAK27112; SynRCC307_0209.
DR   KEGG; syr:SynRCC307_0209; -.
DR   eggNOG; ENOG410689D; Bacteria.
DR   eggNOG; ENOG410XVPP; LUCA.
DR   HOGENOM; HOG000091420; -.
DR   KO; K02708; -.
DR   BioCyc; SSP316278:G1GJL-205-MONOMER; -.
DR   Proteomes; UP000001115; 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:0042651; C: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   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   Pfam; PF00283; Cytochrom_B559; 1.
DR   PIRSF; PIRSF000037; PsbF; 1.
DR   TIGRFAMs; TIGR01333; cyt_b559_beta; 1.
DR   PROSITE; PS00537; CYTOCHROME_B559; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQF3.
DR   SWISS-2DPAGE; A5GQF3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_00643,
KW   ECO:0000256|RuleBase:RU004529};
KW   Heme {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00643,
KW   ECO:0000256|RuleBase:RU004529};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00643,
KW   ECO:0000256|RuleBase:RU004529};
KW   Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00643,
KW   ECO:0000256|RuleBase:RU004529};
KW   Photosystem II {ECO:0000256|HAMAP-Rule:MF_00643,
KW   ECO:0000256|RuleBase:RU004529};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_00643};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00643,
KW   ECO:0000256|RuleBase:RU004529};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00643,
KW   ECO:0000256|RuleBase:RU004529};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00643,
KW   ECO:0000256|RuleBase:RU004529}.
FT   TRANSMEM     20     43       Helical. {ECO:0000256|RuleBase:RU004529}.
FT   DOMAIN        7     35       Cytochrom_B559. {ECO:0000259|Pfam:
FT                                PF00283}.
FT   METAL        24     24       Iron (heme axial ligand); shared with
FT                                alpha subunit. {ECO:0000256|HAMAP-Rule:
FT                                MF_00643}.
SQ   SEQUENCE   45 AA;  5034 MW;  2D04E7AB21673CAD CRC64;
     MTSTPSPATP RNYPIFTVRW LSLHALGIPT VFFLGALAAM QFVRR
//

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