RCEL_BLAVI
ID RCEL_BLAVI Reviewed; 274 AA.
AC P06009;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Reaction center protein L chain;
DE AltName: Full=Photosynthetic reaction center L subunit;
GN Name=pufL;
OS Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19567 / DSM 133 / F;
RX PubMed=15966102; DOI=10.1002/j.1460-2075.1986.tb04340.x;
RA Michel H., Weyer K.A., Gruenberg H., Dunger I., Oesterhelt D.,
RA Lottspeich F.;
RT "The 'light' and 'medium' subunits of the photosynthetic reaction centre
RT from Rhodopseudomonas viridis: isolation of the genes, nucleotide and amino
RT acid sequence.";
RL EMBO J. 5:1149-1158(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RA Deisenhofer J., Epp O., Miki K., Huber R., Michel H.;
RT "Structure of the protein subunits in the photosynthetic reaction centre of
RT Rhodopseudomonas viridis at 3-A resolution.";
RL Nature 318:618-624(1985).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX PubMed=6392571; DOI=10.1016/s0022-2836(84)80011-x;
RA Deisenhofer J., Epp O., Miki K., Huber R., Michel H.;
RT "X-ray structure analysis of a membrane protein complex. Electron density
RT map at 3-A resolution and a model of the chromophores of the photosynthetic
RT reaction center from Rhodopseudomonas viridis.";
RL J. Mol. Biol. 180:385-398(1984).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RC STRAIN=ATCC 19567 / DSM 133 / F;
RX PubMed=9351808; DOI=10.1016/s0969-2126(97)00285-2;
RA Lancaster C.R.D., Michel H.;
RT "The coupling of light-induced electron transfer and proton uptake as
RT derived from crystal structures of reaction centres from Rhodopseudomonas
RT viridis modified at the binding site of the secondary quinone, QB.";
RL Structure 5:1339-1359(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RC STRAIN=ATCC 19567 / DSM 133 / F;
RX PubMed=10024457; DOI=10.1006/jmbi.1998.2532;
RA Lancaster C.R.D., Michel H.;
RT "Refined crystal structures of reaction centres from Rhodopseudomonas
RT viridis in complexes with the herbicide atrazine and two chiral atrazine
RT derivatives also lead to a new model of the bound carotenoid.";
RL J. Mol. Biol. 286:883-898(1999).
RN [6]
RP TOPOLOGY.
RX PubMed=2676514; DOI=10.1002/j.1460-2075.1989.tb08338.x;
RA Deisenhofer J., Michel H.;
RT "Nobel lecture. The photosynthetic reaction centre from the purple
RT bacterium Rhodopseudomonas viridis.";
RL EMBO J. 8:2149-2170(1989).
CC -!- FUNCTION: The reaction center is a membrane-bound complex that mediates
CC the initial photochemical event in the electron transfer process of
CC photosynthesis.
CC -!- SUBUNIT: Reaction center is composed of four bacteriochlorophylls, two
CC bacteriopheophytins, two ubiquinones, one iron, and three highly
CC hydrophobic polypeptide chains (designated L, M, and H).
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000305}.
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DR EMBL; X03915; CAA27550.1; -; Genomic_DNA.
DR PIR; A25102; A25102.
DR RefSeq; WP_055036366.1; NZ_LN907867.1.
DR PDB; 1DXR; X-ray; 2.00 A; L=2-274.
DR PDB; 1PRC; X-ray; 2.30 A; L=2-274.
DR PDB; 1R2C; X-ray; 2.86 A; L=2-274.
DR PDB; 1VRN; X-ray; 2.20 A; L=2-274.
DR PDB; 2I5N; X-ray; 1.96 A; L=2-274.
DR PDB; 2JBL; X-ray; 2.40 A; L=2-274.
DR PDB; 2PRC; X-ray; 2.45 A; L=2-274.
DR PDB; 2WJM; X-ray; 1.95 A; L=1-274.
DR PDB; 2WJN; X-ray; 1.86 A; L=1-274.
DR PDB; 2X5U; X-ray; 3.00 A; L=1-274.
DR PDB; 2X5V; X-ray; 3.00 A; L=1-274.
DR PDB; 3D38; X-ray; 3.21 A; L=2-274.
DR PDB; 3G7F; X-ray; 2.50 A; L=2-274.
DR PDB; 3PRC; X-ray; 2.40 A; L=2-274.
DR PDB; 3T6D; X-ray; 1.95 A; L=2-274.
DR PDB; 3T6E; X-ray; 1.92 A; L=2-274.
DR PDB; 4AC5; X-ray; 8.20 A; L=1-274.
DR PDB; 4CAS; X-ray; 3.50 A; B=1-274.
DR PDB; 5M7J; X-ray; 3.50 A; B=1-274.
DR PDB; 5M7K; X-ray; 3.50 A; B=1-274.
DR PDB; 5M7L; X-ray; 3.60 A; B=1-274.
DR PDB; 5NJ4; X-ray; 2.40 A; L=2-274.
DR PDB; 5O4C; X-ray; 2.80 A; L=2-274.
DR PDB; 5O64; X-ray; 3.30 A; L=2-274.
DR PDB; 5PRC; X-ray; 2.35 A; L=2-274.
DR PDB; 6ET5; EM; 3.00 A; L=1-274.
DR PDB; 6PRC; X-ray; 2.30 A; L=2-274.
DR PDB; 6ZHW; X-ray; 2.80 A; L=2-274.
DR PDB; 6ZI4; X-ray; 2.80 A; L=2-274.
DR PDB; 6ZI5; X-ray; 2.80 A; L=2-274.
DR PDB; 6ZI6; X-ray; 2.80 A; L=2-274.
DR PDB; 6ZI9; X-ray; 2.80 A; L=2-274.
DR PDB; 6ZIA; X-ray; 2.80 A; L=2-274.
DR PDB; 6ZID; X-ray; 2.80 A; L=2-274.
DR PDB; 7PRC; X-ray; 2.65 A; L=2-274.
DR PDBsum; 1DXR; -.
DR PDBsum; 1PRC; -.
DR PDBsum; 1R2C; -.
DR PDBsum; 1VRN; -.
DR PDBsum; 2I5N; -.
DR PDBsum; 2JBL; -.
DR PDBsum; 2PRC; -.
DR PDBsum; 2WJM; -.
DR PDBsum; 2WJN; -.
DR PDBsum; 2X5U; -.
DR PDBsum; 2X5V; -.
DR PDBsum; 3D38; -.
DR PDBsum; 3G7F; -.
DR PDBsum; 3PRC; -.
DR PDBsum; 3T6D; -.
DR PDBsum; 3T6E; -.
DR PDBsum; 4AC5; -.
DR PDBsum; 4CAS; -.
DR PDBsum; 5M7J; -.
DR PDBsum; 5M7K; -.
DR PDBsum; 5M7L; -.
DR PDBsum; 5NJ4; -.
DR PDBsum; 5O4C; -.
DR PDBsum; 5O64; -.
DR PDBsum; 5PRC; -.
DR PDBsum; 6ET5; -.
DR PDBsum; 6PRC; -.
DR PDBsum; 6ZHW; -.
DR PDBsum; 6ZI4; -.
DR PDBsum; 6ZI5; -.
DR PDBsum; 6ZI6; -.
DR PDBsum; 6ZI9; -.
DR PDBsum; 6ZIA; -.
DR PDBsum; 6ZID; -.
DR PDBsum; 7PRC; -.
DR AlphaFoldDB; P06009; -.
DR SMR; P06009; -.
DR IntAct; P06009; 1.
DR STRING; 1079.BVIR_604; -.
DR DrugBank; DB07552; (2R)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile.
DR DrugBank; DB07551; (2S)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile.
DR DrugBank; DB07392; Atrazine.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB04464; N-Formylmethionine.
DR DrugBank; DB08215; Terbutryn.
DR DrugBank; DB08689; Ubiquinone Q1.
DR DrugBank; DB08690; Ubiquinone Q2.
DR OMA; WGHGFPY; -.
DR OrthoDB; 529504at2; -.
DR EvolutionaryTrace; P06009; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042314; F:bacteriochlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR CDD; cd09290; Photo-RC_L; 1.
DR Gene3D; 1.20.85.10; -; 2.
DR InterPro; IPR036854; Photo_II_D1/D2_sf.
DR InterPro; IPR005871; Photo_RC_L.
DR InterPro; IPR000484; Photo_RC_L/M.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; SSF81483; 1.
DR TIGRFAMs; TIGR01157; pufL; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacteriochlorophyll; Chlorophyll; Chromophore;
KW Electron transport; Iron; Magnesium; Membrane; Metal-binding;
KW Photosynthesis; Reaction center; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..274
FT /note="Reaction center protein L chain"
FT /id="PRO_0000090410"
FT TOPO_DOM 2..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 33..53
FT /note="Helical"
FT TOPO_DOM 54..83
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 84..111
FT /note="Helical"
FT TOPO_DOM 112..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 116..139
FT /note="Helical"
FT TOPO_DOM 140..170
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 171..198
FT /note="Helical"
FT TOPO_DOM 199..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 226..249
FT /note="Helical"
FT TOPO_DOM 250..274
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT BINDING 154
FT /ligand="(7R,8Z)-bacteriochlorophyll b"
FT /ligand_id="ChEBI:CHEBI:30034"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT BINDING 174
FT /ligand="(7R,8Z)-bacteriochlorophyll b"
FT /ligand_id="ChEBI:CHEBI:30034"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 217
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6PRC"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:5O64"
FT HELIX 33..55
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3PRC"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 85..111
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 172..199
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 229..251
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2WJN"
SQ SEQUENCE 274 AA; 30578 MW; 98E0F11A7345EC38 CRC64;
MALLSFERKY RVRGGTLIGG DLFDFWVGPY FVGFFGVSAI FFIFLGVSLI GYAASQGPTW
DPFAISINPP DLKYGLGAAP LLEGGFWQAI TVCALGAFIS WMLREVEISR KLGIGWHVPL
AFCVPIFMFC VLQVFRPLLL GSWGHAFPYG ILSHLDWVNN FGYQYLNWHY NPGHMSSVSF
LFVNAMALGL HGGLILSVAN PGDGDKVKTA EHENQYFRDV VGYSIGALSI HRLGLFLASN
IFLTGAFGTI ASGPFWTRGW PEWWGWWLDI PFWS
