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PSBF_HORVU
ID   PSBF_HORVU              Reviewed;          39 AA.
AC   P60126; A1E9K6; P05171; P09198; Q95H58; Q9M3L1;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Cytochrome b559 subunit beta {ECO:0000255|HAMAP-Rule:MF_00643};
DE   AltName: Full=PSII reaction center subunit VI {ECO:0000255|HAMAP-Rule:MF_00643};
GN   Name=psbF {ECO:0000255|HAMAP-Rule:MF_00643};
OS   Hordeum vulgare (Barley).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Sabarlis;
RX   PubMed=2654886; DOI=10.1093/nar/17.7.2858;
RA   Chakhmakhcheva O.G., Andreeva A.V., Buryakova A.A., Reverdatto S.V.,
RA   Efimov V.A.;
RT   "Nucleotide sequence of the barley chloroplast psbE, psbF genes and
RT   flanking regions.";
RL   Nucleic Acids Res. 17:2858-2858(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Sabarlis;
RX   PubMed=1804121;
RA   Efimov V.A., Andreeva A.V., Reverdatto S.V., Chakhmakhcheva O.G.;
RT   "Photosystem II of rye. Nucleotide sequence of the psbB, psbC, psbE, psbF,
RT   psbH genes of rye and chloroplast DNA regions adjacent to them.";
RL   Bioorg. Khim. 17:1369-1385(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3256307; DOI=10.1007/bf02908413;
RA   Krupinska K., Berry-Lowe S.;
RT   "Characterization and in vitro expression of the cytochrome b-559 genes of
RT   barley. I. Localization and sequence of the genes.";
RL   Carlsberg Res. Commun. 53:43-55(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex;
RX   PubMed=17534593; DOI=10.1007/s00122-007-0567-4;
RA   Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H.,
RA   Tomkins J., Rognli O.A., Daniell H., Clarke J.L.;
RT   "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor
RT   and Agrostis stolonifera, and comparative analyses with other grass
RT   genomes.";
RL   Theor. Appl. Genet. 115:571-590(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Steffi;
RX   PubMed=19137553; DOI=10.1002/pmic.200800337;
RA   Ploescher M., Granvogl B., Zoryan M., Reisinger V., Eichacker L.A.;
RT   "Mass spectrometric characterization of membrane integral low molecular
RT   weight proteins from photosystem II in barley etioplasts.";
RL   Proteomics 9:625-635(2009).
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_00643}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00643};
CC       Note=With its partner (PsbE) binds heme. PSII binds additional
CC       chlorophylls, carotenoids and specific lipids. {ECO:0000255|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       Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex
CC       and a large number of cofactors. It forms dimeric complexes (By
CC       similarity). Detected in both etioplasts and green leaves; PSII is only
CC       assembled in green leaves (PubMed:19137553). {ECO:0000255|HAMAP-
CC       Rule:MF_00643, ECO:0000269|PubMed:19137553}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000305|PubMed:19137553}; Single-
CC       pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00643,
CC       ECO:0000305|PubMed:19137553}.
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00643}.
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DR   EMBL; X14108; CAA32271.1; -; Genomic_DNA.
DR   EMBL; M35616; AAA84049.1; -; Genomic_DNA.
DR   EMBL; M35977; AAA84045.1; -; Genomic_DNA.
DR   EMBL; EF115541; ABK79428.1; -; Genomic_DNA.
DR   PIR; S04063; S04063.
DR   RefSeq; YP_874668.1; NC_008590.1.
DR   AlphaFoldDB; P60126; -.
DR   SMR; P60126; -.
DR   GeneID; 4525054; -.
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   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   PANTHER; PTHR33391:SF14; PTHR33391:SF14; 1.
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   1: Evidence at protein level;
KW   Chloroplast; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Photosynthesis; Photosystem II; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..39
FT                   /note="Cytochrome b559 subunit beta"
FT                   /id="PRO_0000200397"
FT   TRANSMEM        14..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00643"
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:0000255|HAMAP-Rule:MF_00643"
SQ   SEQUENCE   39 AA;  4498 MW;  591251852D6E0A03 CRC64;
     MTIDRTYPIF TVRWLAIHGL AVPTVFFLGS ISAMQFIQR
 
 
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