RCEL_RHORU
ID RCEL_RHORU Reviewed; 276 AA.
AC P10717;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Reaction center protein L chain;
DE AltName: Full=Photosynthetic reaction center L subunit;
GN Name=pufL;
OS Rhodospirillum rubrum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=1085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2836391; DOI=10.1016/s0021-9258(18)68545-x;
RA Belanger G., Berard J., Corriveau P., Gingras G.;
RT "The structural genes coding for the L and M subunits of Rhodospirillum
RT rubrum photoreaction center.";
RL J. Biol. Chem. 263:7632-7638(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-37.
RX PubMed=6199280; DOI=10.1515/bchm2.1983.364.2.1765;
RA Theiler R., Suter F., Zuber H.;
RT "N-terminal sequences of subunits L and M of the photosynthetic reaction
RT centre from Rhodospirillum rubrum G-9+. Separation of the subunits by gel
RT filtration on hydroxypropylated Sephadex G 100 in organic solvents.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:1765-1776(1983).
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; J03731; AAA26464.1; -; Genomic_DNA.
DR PIR; A28170; A28170.
DR RefSeq; WP_011390723.1; NZ_NHSM01000198.1.
DR PDB; 7EQD; EM; 2.76 A; L=2-276.
DR PDBsum; 7EQD; -.
DR AlphaFoldDB; P10717; -.
DR SMR; P10717; -.
DR OMA; WGHGFPY; -.
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 Direct protein sequencing; Electron transport; Iron; Magnesium; Membrane;
KW Metal-binding; Photosynthesis; Reaction center; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6199280"
FT CHAIN 2..276
FT /note="Reaction center protein L chain"
FT /id="PRO_0000090409"
FT TRANSMEM 33..56
FT /note="Helical"
FT TRANSMEM 85..113
FT /note="Helical"
FT TRANSMEM 116..141
FT /note="Helical"
FT TRANSMEM 171..200
FT /note="Helical"
FT TRANSMEM 226..252
FT /note="Helical"
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..9
FT /evidence="ECO:0007829|PDB:7EQD"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 33..56
FT /evidence="ECO:0007829|PDB:7EQD"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:7EQD"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 85..112
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 172..199
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 229..251
FT /evidence="ECO:0007829|PDB:7EQD"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:7EQD"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:7EQD"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:7EQD"
SQ SEQUENCE 276 AA; 30640 MW; DFAB5FFA03F71735 CRC64;
MALLSFERKY RVRGGTLIGG DLFDFWVGPF YVGFFGVTTL LFTVLGTALI VWGAALGPSW
TFWQISINPP DVSYGLAMAP MAKGGLWQII TFSAIGAFVS WALREVEICR KLGIGYHIPF
AFGFAILAYV SLVVIRPVMM GAWGYGFPYG FMTHLDWVSN TGYQYANFHY NPAHMLGITL
FFTTCLALAL HGSLILSAAN PGKGEVVKGP EHENTYFQDT IGYSVGTLGI HRVGLILALS
AVVWSIICMI LSGPIYTGSW PDWWLWWQKL PFWNHG
