RCEL_CERSP
ID RCEL_CERSP Reviewed; 282 AA.
AC P0C0Y8; P02954; Q9RFB9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Reaction center protein L chain;
DE AltName: Full=Photosynthetic reaction center L subunit;
GN Name=pufL;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6095283; DOI=10.1073/pnas.81.23.7303;
RA Williams J.C., Steiner L.A., Feher G., Simon M.I.;
RT "Primary structure of the L subunit of the reaction center from
RT Rhodopseudomonas sphaeroides.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7303-7307(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Y;
RX PubMed=2126457; DOI=10.1016/0300-9084(90)90116-x;
RA Arnoux B., Ducruix A., Astier C., Picaud M., Roth M., Reiss-Husson F.;
RT "Towards the understanding of the function of Rb sphaeroides Y wild type
RT reaction center: gene cloning, protein and detergent structures in the
RT three-dimensional crystals.";
RL Biochimie 72:525-530(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
RX PubMed=2036404; DOI=10.1021/bi00236a005;
RA Chang C.-H., El-Kabbani O., Tiede D., Norris J., Schiffer M.;
RT "Structure of the membrane-bound protein photosynthetic reaction center
RT from Rhodobacter sphaeroides.";
RL Biochemistry 30:5352-5360(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC STRAIN=R-26;
RX PubMed=3054889; DOI=10.1073/pnas.85.22.8487;
RA Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.;
RT "Structure of the reaction center from Rhodobacter sphaeroides R-26:
RT protein-cofactor (quinones and Fe2+) interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8487-8491(1988).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC STRAIN=R-26;
RX PubMed=2819866; DOI=10.1073/pnas.84.17.6162;
RA Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.;
RT "Structure of the reaction center from Rhodobacter sphaeroides R-26: the
RT protein subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6162-6166(1987).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
RX PubMed=9537989; DOI=10.1021/bi971717a;
RA McAuley-Hecht K.E., Fyfe P.K., Ridge J.P., Prince S.M., Hunter C.N.,
RA Isaacs N.W., Cogdell R.J., Jones M.R.;
RT "Structural studies of wild-type and mutant reaction centers from an
RT antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical
RT properties of the complex from bacterial cell to crystal.";
RL Biochemistry 37:4740-4750(1998).
RN [7]
RP TOPOLOGY.
RX PubMed=1645718; DOI=10.1016/s0021-9258(18)99114-3;
RA Yun C.H., Van Doren S.R., Crofts A.R., Gennis R.B.;
RT "The use of gene fusions to examine the membrane topology of the L-subunit
RT of the photosynthetic reaction center and of the cytochrome b subunit of
RT the bc1 complex from Rhodobacter sphaeroides.";
RL J. Biol. Chem. 266:10967-10973(1991).
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; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000305}.
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DR EMBL; M10206; AAA26177.1; -; Genomic_DNA.
DR EMBL; X63404; CAA44999.1; -; Genomic_DNA.
DR PIR; S24212; WNRFLS.
DR RefSeq; WP_002720421.1; NZ_WTFI01000042.1.
DR PDB; 1AIG; X-ray; 2.60 A; L/N=2-282.
DR PDB; 1AIJ; X-ray; 2.20 A; L/R=2-282.
DR PDB; 1DS8; X-ray; 2.50 A; L/R=2-282.
DR PDB; 1DV3; X-ray; 2.50 A; L/R=2-282.
DR PDB; 1DV6; X-ray; 2.50 A; L/R=2-282.
DR PDB; 1E14; X-ray; 2.70 A; L=2-282.
DR PDB; 1E6D; X-ray; 2.30 A; L=2-282.
DR PDB; 1F6N; X-ray; 2.80 A; L=2-282.
DR PDB; 1FNP; X-ray; 2.60 A; L=2-282.
DR PDB; 1FNQ; X-ray; 2.60 A; L=2-282.
DR PDB; 1JGW; X-ray; 2.80 A; L=2-282.
DR PDB; 1JGX; X-ray; 3.01 A; L=2-282.
DR PDB; 1JGY; X-ray; 2.70 A; L=2-282.
DR PDB; 1JGZ; X-ray; 2.70 A; L=2-282.
DR PDB; 1JH0; X-ray; 3.50 A; L=2-282.
DR PDB; 1K6L; X-ray; 3.10 A; L=2-282.
DR PDB; 1K6N; X-ray; 3.10 A; L=2-282.
DR PDB; 1KBY; X-ray; 2.50 A; L=2-282.
DR PDB; 1L9B; X-ray; 2.40 A; L=2-282.
DR PDB; 1L9J; X-ray; 3.25 A; L/R=2-282.
DR PDB; 1M3X; X-ray; 2.55 A; L=2-282.
DR PDB; 1MPS; X-ray; 2.55 A; L=2-282.
DR PDB; 1OGV; X-ray; 2.35 A; L=2-282.
DR PDB; 1PCR; X-ray; 2.65 A; L=2-282.
DR PDB; 1PSS; X-ray; 3.00 A; L=6-271.
DR PDB; 1PST; X-ray; 3.00 A; L=6-271.
DR PDB; 1QOV; X-ray; 2.10 A; L=2-282.
DR PDB; 1RG5; X-ray; 2.50 A; L=2-282.
DR PDB; 1RGN; X-ray; 2.80 A; L=2-282.
DR PDB; 1RQK; X-ray; 2.70 A; L=2-282.
DR PDB; 1RVJ; X-ray; 2.75 A; L=2-282.
DR PDB; 1RY5; X-ray; 2.10 A; L=2-282.
DR PDB; 1RZH; X-ray; 1.80 A; L=2-282.
DR PDB; 1RZZ; X-ray; 2.40 A; L/R=2-282.
DR PDB; 1S00; X-ray; 2.60 A; L/R=2-282.
DR PDB; 1UMX; X-ray; 2.80 A; L=2-282.
DR PDB; 1YF6; X-ray; 2.25 A; L=2-282.
DR PDB; 1YST; X-ray; 3.00 A; L=2-274.
DR PDB; 1Z9J; X-ray; 4.50 A; A=2-282.
DR PDB; 1Z9K; X-ray; 4.60 A; A=2-282.
DR PDB; 2BNP; X-ray; 2.70 A; A=2-282.
DR PDB; 2BNS; X-ray; 2.50 A; A=2-282.
DR PDB; 2BOZ; X-ray; 2.40 A; L=2-282.
DR PDB; 2GMR; X-ray; 2.50 A; L=2-282.
DR PDB; 2GNU; X-ray; 2.20 A; L=2-282.
DR PDB; 2HG3; X-ray; 2.70 A; L=2-282.
DR PDB; 2HG9; X-ray; 2.45 A; L=2-282.
DR PDB; 2HH1; X-ray; 2.55 A; L=2-282.
DR PDB; 2HHK; X-ray; 2.50 A; L=2-282.
DR PDB; 2HIT; X-ray; 2.75 A; L=2-282.
DR PDB; 2HJ6; X-ray; 3.00 A; L=2-282.
DR PDB; 2J8C; X-ray; 1.87 A; L=2-282.
DR PDB; 2J8D; X-ray; 2.07 A; L=2-282.
DR PDB; 2JIY; X-ray; 2.20 A; L=2-282.
DR PDB; 2JJ0; X-ray; 2.80 A; L=2-282.
DR PDB; 2RCR; X-ray; 3.10 A; L=2-282.
DR PDB; 2UWS; X-ray; 2.90 A; L=2-282.
DR PDB; 2UWT; X-ray; 2.50 A; L=2-282.
DR PDB; 2UWU; X-ray; 2.04 A; L=2-282.
DR PDB; 2UWV; X-ray; 2.13 A; L=2-282.
DR PDB; 2UWW; X-ray; 2.05 A; L=2-282.
DR PDB; 2UX3; X-ray; 2.50 A; L=2-282.
DR PDB; 2UX4; X-ray; 2.51 A; L=2-282.
DR PDB; 2UX5; X-ray; 2.21 A; L=2-282.
DR PDB; 2UXJ; X-ray; 2.25 A; L=2-282.
DR PDB; 2UXK; X-ray; 2.31 A; L=2-282.
DR PDB; 2UXL; X-ray; 2.88 A; L=2-282.
DR PDB; 2UXM; X-ray; 2.70 A; L=2-282.
DR PDB; 3DSY; X-ray; 3.00 A; L=2-282.
DR PDB; 3DTA; X-ray; 3.20 A; L=2-282.
DR PDB; 3DTR; X-ray; 3.10 A; L=2-282.
DR PDB; 3DTS; X-ray; 3.10 A; L=2-282.
DR PDB; 3DU2; X-ray; 3.10 A; L=2-282.
DR PDB; 3DU3; X-ray; 2.80 A; L=2-282.
DR PDB; 3DUQ; X-ray; 2.70 A; L=2-282.
DR PDB; 3I4D; X-ray; 2.01 A; L=2-282.
DR PDB; 3V3Y; X-ray; 2.80 A; L=2-282.
DR PDB; 3V3Z; X-ray; 2.90 A; L=2-282.
DR PDB; 3ZUM; X-ray; 2.50 A; L=2-282.
DR PDB; 3ZUW; X-ray; 2.31 A; L=2-282.
DR PDB; 4H99; X-ray; 2.97 A; L=2-282.
DR PDB; 4H9L; X-ray; 2.77 A; L=2-282.
DR PDB; 4HBH; X-ray; 2.93 A; L=2-282.
DR PDB; 4HBJ; X-ray; 2.74 A; L=2-282.
DR PDB; 4IN7; X-ray; 2.85 A; L=2-282.
DR PDB; 4LWY; X-ray; 2.90 A; L=1-282.
DR PDB; 4N7K; X-ray; 2.85 A; L=2-282.
DR PDB; 4RCR; X-ray; 2.80 A; L=2-282.
DR PDB; 4TQQ; X-ray; 2.50 A; L=2-282.
DR PDB; 4V9G; X-ray; 7.78 A; AL/BL=1-282.
DR PDB; 5LSE; X-ray; 2.50 A; L=2-282.
DR PDB; 5V33; X-ray; 3.49 A; L=2-282.
DR PDB; 6Z02; X-ray; 2.10 A; L=2-282.
DR PDB; 6Z1J; X-ray; 2.10 A; L=2-282.
DR PDB; 6Z27; X-ray; 2.10 A; L=2-282.
DR PDB; 7MH3; X-ray; 2.30 A; L=1-282.
DR PDB; 7MH4; X-ray; 2.48 A; L=1-282.
DR PDB; 7MH5; X-ray; 2.85 A; L=1-282.
DR PDB; 7MH8; X-ray; 2.75 A; L=1-282.
DR PDB; 7MH9; X-ray; 3.10 A; L=1-282.
DR PDBsum; 1AIG; -.
DR PDBsum; 1AIJ; -.
DR PDBsum; 1DS8; -.
DR PDBsum; 1DV3; -.
DR PDBsum; 1DV6; -.
DR PDBsum; 1E14; -.
DR PDBsum; 1E6D; -.
DR PDBsum; 1F6N; -.
DR PDBsum; 1FNP; -.
DR PDBsum; 1FNQ; -.
DR PDBsum; 1JGW; -.
DR PDBsum; 1JGX; -.
DR PDBsum; 1JGY; -.
DR PDBsum; 1JGZ; -.
DR PDBsum; 1JH0; -.
DR PDBsum; 1K6L; -.
DR PDBsum; 1K6N; -.
DR PDBsum; 1KBY; -.
DR PDBsum; 1L9B; -.
DR PDBsum; 1L9J; -.
DR PDBsum; 1M3X; -.
DR PDBsum; 1MPS; -.
DR PDBsum; 1OGV; -.
DR PDBsum; 1PCR; -.
DR PDBsum; 1PSS; -.
DR PDBsum; 1PST; -.
DR PDBsum; 1QOV; -.
DR PDBsum; 1RG5; -.
DR PDBsum; 1RGN; -.
DR PDBsum; 1RQK; -.
DR PDBsum; 1RVJ; -.
DR PDBsum; 1RY5; -.
DR PDBsum; 1RZH; -.
DR PDBsum; 1RZZ; -.
DR PDBsum; 1S00; -.
DR PDBsum; 1UMX; -.
DR PDBsum; 1YF6; -.
DR PDBsum; 1YST; -.
DR PDBsum; 1Z9J; -.
DR PDBsum; 1Z9K; -.
DR PDBsum; 2BNP; -.
DR PDBsum; 2BNS; -.
DR PDBsum; 2BOZ; -.
DR PDBsum; 2GMR; -.
DR PDBsum; 2GNU; -.
DR PDBsum; 2HG3; -.
DR PDBsum; 2HG9; -.
DR PDBsum; 2HH1; -.
DR PDBsum; 2HHK; -.
DR PDBsum; 2HIT; -.
DR PDBsum; 2HJ6; -.
DR PDBsum; 2J8C; -.
DR PDBsum; 2J8D; -.
DR PDBsum; 2JIY; -.
DR PDBsum; 2JJ0; -.
DR PDBsum; 2RCR; -.
DR PDBsum; 2UWS; -.
DR PDBsum; 2UWT; -.
DR PDBsum; 2UWU; -.
DR PDBsum; 2UWV; -.
DR PDBsum; 2UWW; -.
DR PDBsum; 2UX3; -.
DR PDBsum; 2UX4; -.
DR PDBsum; 2UX5; -.
DR PDBsum; 2UXJ; -.
DR PDBsum; 2UXK; -.
DR PDBsum; 2UXL; -.
DR PDBsum; 2UXM; -.
DR PDBsum; 3DSY; -.
DR PDBsum; 3DTA; -.
DR PDBsum; 3DTR; -.
DR PDBsum; 3DTS; -.
DR PDBsum; 3DU2; -.
DR PDBsum; 3DU3; -.
DR PDBsum; 3DUQ; -.
DR PDBsum; 3I4D; -.
DR PDBsum; 3V3Y; -.
DR PDBsum; 3V3Z; -.
DR PDBsum; 3ZUM; -.
DR PDBsum; 3ZUW; -.
DR PDBsum; 4H99; -.
DR PDBsum; 4H9L; -.
DR PDBsum; 4HBH; -.
DR PDBsum; 4HBJ; -.
DR PDBsum; 4IN7; -.
DR PDBsum; 4LWY; -.
DR PDBsum; 4N7K; -.
DR PDBsum; 4RCR; -.
DR PDBsum; 4TQQ; -.
DR PDBsum; 4V9G; -.
DR PDBsum; 5LSE; -.
DR PDBsum; 5V33; -.
DR PDBsum; 6Z02; -.
DR PDBsum; 6Z1J; -.
DR PDBsum; 6Z27; -.
DR PDBsum; 7MH3; -.
DR PDBsum; 7MH4; -.
DR PDBsum; 7MH5; -.
DR PDBsum; 7MH8; -.
DR PDBsum; 7MH9; -.
DR AlphaFoldDB; P0C0Y8; -.
DR SMR; P0C0Y8; -.
DR DIP; DIP-60489N; -.
DR IntAct; P0C0Y8; 1.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB08215; Terbutryn.
DR DrugBank; DB08690; Ubiquinone Q2.
DR TCDB; 3.E.2.1.1; the photosynthetic reaction center (prc) family.
DR GeneID; 57470575; -.
DR GeneID; 67446990; -.
DR OMA; WGHGFPY; -.
DR OrthoDB; 529504at2; -.
DR EvolutionaryTrace; P0C0Y8; -.
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..282
FT /note="Reaction center protein L chain"
FT /id="PRO_0000090407"
FT TOPO_DOM 2..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1645718"
FT TRANSMEM 33..56
FT /note="Helical"
FT TOPO_DOM 57..83
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:1645718"
FT TRANSMEM 84..112
FT /note="Helical"
FT TOPO_DOM 113..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1645718"
FT TRANSMEM 117..139
FT /note="Helical"
FT TOPO_DOM 140..171
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:1645718"
FT TRANSMEM 172..199
FT /note="Helical"
FT TOPO_DOM 200..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1645718"
FT TRANSMEM 226..251
FT /note="Helical"
FT TOPO_DOM 252..282
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:1645718"
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:1RZH"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1RZH"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1KBY"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1KBY"
FT HELIX 33..57
FT /evidence="ECO:0007829|PDB:1RZH"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 85..112
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 172..199
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1PCR"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 227..250
FT /evidence="ECO:0007829|PDB:1RZH"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:1RZH"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:1RZH"
FT TURN 271..275
FT /evidence="ECO:0007829|PDB:1RZH"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1RZH"
SQ SEQUENCE 282 AA; 31457 MW; 044F4D3AF085B136 CRC64;
MALLSFERKY RVPGGTLVGG NLFDFWVGPF YVGFFGVATF FFAALGIILI AWSAVLQGTW
NPQLISVYPP ALEYGLGGAP LAKGGLWQII TICATGAFVS WALREVEICR KLGIGYHIPF
AFAFAILAYL TLVLFRPVMM GAWGYAFPYG IWTHLDWVSN TGYTYGNFHY NPAHMIAISF
FFTNALALAL HGALVLSAAN PEKGKEMRTP DHEDTFFRDL VGYSIGTLGI HRLGLLLSLS
AVFFSALCMI ITGTIWFDQW VDWWQWWVKL PWWANIPGGI NG
