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PSBF_THEVL
ID   PSBF_THEVL              Reviewed;          45 AA.
AC   P12239; Q8GI49;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 112.
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   Thermostichus vulcanus (Synechococcus vulcanus).
OC   Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX   NCBI_TaxID=32053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, COMPOSITION OF
RP   PHOTOSYSTEM II, AND SUBUNIT.
RX   PubMed=12461137; DOI=10.1093/pcp/pcf168;
RA   Kashino Y., Koike H., Yoshio M., Egashira H., Ikeuchi M., Pakrasi H.B.,
RA   Satoh K.;
RT   "Low-molecular-mass polypeptide components of a photosystem II preparation
RT   from the thermophilic cyanobacterium Thermosynechococcus vulcanus.";
RL   Plant Cell Physiol. 43:1366-1373(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-22.
RX   DOI=10.1016/0014-5793(89)81446-2;
RA   Ikeuchi M., Koike H., Inoue Y.;
RT   "Identification of psbI and psbL gene products in cyanobacterial
RT   photosystem II reaction center preparation.";
RL   FEBS Lett. 251:155-160(1989).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 2-45 IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=12518057; DOI=10.1073/pnas.0135651100;
RA   Kamiya N., Shen J.-R.;
RT   "Crystal structure of oxygen-evolving photosystem II from
RT   Thermosynechococcus vulcanus at 3.7-A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:98-103(2003).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 2-45 IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=19433803; DOI=10.1073/pnas.0812797106;
RA   Kawakami K., Umena Y., Kamiya N., Shen J.R.;
RT   "Location of chloride and its possible functions in oxygen-evolving
RT   photosystem II revealed by X-ray crystallography.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8567-8572(2009).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-45 IN COMPLEX WITH HEME IN
RP   PHOTOSYSTEM II, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=21499260; DOI=10.1038/nature09913;
RA   Umena Y., Kawakami K., Shen J.R., Kamiya N.;
RT   "Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9
RT   A.";
RL   Nature 473:55-60(2011).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-45 IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=23426624; DOI=10.1073/pnas.1219922110;
RA   Koua F.H., Umena Y., Kawakami K., Shen J.R.;
RT   "Structure of Sr-substituted photosystem II at 2.1 A resolution and its
RT   implications in the mechanism of water oxidation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:3889-3894(2013).
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, ECO:0000269|PubMed:19433803,
CC       ECO:0000269|PubMed:23426624}.
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, ECO:0000269|PubMed:12518057,
CC       ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC       ECO:0000269|PubMed:23426624};
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_00643, ECO:0000269|PubMed:12461137,
CC       ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC       ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00643, ECO:0000269|PubMed:12518057,
CC       ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC       ECO:0000269|PubMed:23426624}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:12518057,
CC       ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC       ECO:0000269|PubMed:23426624}.
CC   -!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00643}.
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DR   EMBL; AB086860; BAC53635.1; -; Genomic_DNA.
DR   PIR; S05031; S05031.
DR   PDB; 1IZL; X-ray; 3.70 A; F/Q=2-45.
DR   PDB; 3A0B; X-ray; 3.70 A; F/f=2-45.
DR   PDB; 3A0H; X-ray; 4.00 A; F/f=2-45.
DR   PDB; 3WU2; X-ray; 1.90 A; F/f=2-45.
DR   PDB; 4IL6; X-ray; 2.10 A; F/f=12-45.
DR   PDB; 4UB6; X-ray; 1.95 A; F/f=2-45.
DR   PDB; 4UB8; X-ray; 1.95 A; F/f=2-45.
DR   PDB; 5B5E; X-ray; 1.87 A; F/f=2-45.
DR   PDB; 5B66; X-ray; 1.85 A; F/f=2-45.
DR   PDB; 5GTH; X-ray; 2.50 A; F/f=2-45.
DR   PDB; 5GTI; X-ray; 2.50 A; F/f=2-45.
DR   PDB; 5V2C; X-ray; 1.90 A; F/f=2-45.
DR   PDB; 5WS5; X-ray; 2.35 A; F/f=2-45.
DR   PDB; 5WS6; X-ray; 2.35 A; F/f=2-45.
DR   PDB; 6JLJ; X-ray; 2.15 A; F/f=2-45.
DR   PDB; 6JLK; X-ray; 2.15 A; F/f=2-45.
DR   PDB; 6JLL; X-ray; 2.15 A; F/f=2-45.
DR   PDB; 6JLM; X-ray; 2.35 A; F/f=2-45.
DR   PDB; 6JLN; X-ray; 2.40 A; F/f=2-45.
DR   PDB; 6JLO; X-ray; 2.40 A; F/f=2-45.
DR   PDB; 6JLP; X-ray; 2.50 A; F/f=2-45.
DR   PDB; 7CJI; X-ray; 2.35 A; F/f=2-45.
DR   PDB; 7CJJ; X-ray; 2.40 A; F/f=2-45.
DR   PDB; 7COU; X-ray; 2.25 A; F/f=2-45.
DR   PDB; 7CZL; EM; 3.78 A; F/f=14-44.
DR   PDB; 7D1T; EM; 1.95 A; F/f=12-45.
DR   PDB; 7D1U; EM; 2.08 A; F/f=12-45.
DR   PDB; 7DXA; EM; 3.14 A; f=1-45.
DR   PDB; 7DXH; EM; 3.14 A; f=1-45.
DR   PDB; 7EDA; EM; 2.78 A; F=1-45.
DR   PDBsum; 1IZL; -.
DR   PDBsum; 3A0B; -.
DR   PDBsum; 3A0H; -.
DR   PDBsum; 3WU2; -.
DR   PDBsum; 4IL6; -.
DR   PDBsum; 4UB6; -.
DR   PDBsum; 4UB8; -.
DR   PDBsum; 5B5E; -.
DR   PDBsum; 5B66; -.
DR   PDBsum; 5GTH; -.
DR   PDBsum; 5GTI; -.
DR   PDBsum; 5V2C; -.
DR   PDBsum; 5WS5; -.
DR   PDBsum; 5WS6; -.
DR   PDBsum; 6JLJ; -.
DR   PDBsum; 6JLK; -.
DR   PDBsum; 6JLL; -.
DR   PDBsum; 6JLM; -.
DR   PDBsum; 6JLN; -.
DR   PDBsum; 6JLO; -.
DR   PDBsum; 6JLP; -.
DR   PDBsum; 7CJI; -.
DR   PDBsum; 7CJJ; -.
DR   PDBsum; 7COU; -.
DR   PDBsum; 7CZL; -.
DR   PDBsum; 7D1T; -.
DR   PDBsum; 7D1U; -.
DR   PDBsum; 7DXA; -.
DR   PDBsum; 7DXH; -.
DR   PDBsum; 7EDA; -.
DR   AlphaFoldDB; P12239; -.
DR   SMR; P12239; -.
DR   DIP; DIP-48863N; -.
DR   IntAct; P12239; 1.
DR   EvolutionaryTrace; P12239; -.
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   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   3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Membrane; Metal-binding; Photosynthesis; Photosystem II; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12461137, ECO:0000269|Ref.2"
FT   CHAIN           2..45
FT                   /note="Cytochrome b559 subunit beta"
FT                   /id="PRO_0000200477"
FT   TOPO_DOM        2..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:21499260"
FT   TRANSMEM        20..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00643,
FT                   ECO:0000269|PubMed:21499260"
FT   TOPO_DOM        37..45
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:21499260"
FT   BINDING         24
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,
FT                   ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624,
FT                   ECO:0000303|PubMed:19433803"
FT   HELIX           18..40
FT                   /evidence="ECO:0007829|PDB:5B66"
SQ   SEQUENCE   45 AA;  5065 MW;  C8D3083549A696C0 CRC64;
     MTSNTPNQEP VSYPIFTVRW VAVHTLAVPT IFFLGAIAAM QFIQR
 
 
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