RCEL_RUBGE
ID RCEL_RUBGE Reviewed; 279 AA.
AC P0DJO2; P51760;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Reaction center protein L chain;
DE AltName: Full=Photosynthetic reaction center L subunit;
GN Name=pufL;
OS Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS gelatinosa).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=28068;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HERBICIDE RESISTANT.
RC STRAIN=S1;
RX PubMed=7589500; DOI=10.1016/0014-5793(95)01055-j;
RA Ouchane S., Picaud M., Astier C.;
RT "A new mutation in the pufL gene responsible for the terbutryn resistance
RT phenotype in Rubrivivax gelatinosus.";
RL FEBS Lett. 374:130-134(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1;
RX PubMed=8879238; DOI=10.1007/bf02173002;
RA Ouchane S., Picaud M., Reiss-Husson F., Vernotte C., Astier C.;
RT "Development of gene transfer methods for Rubrivivax gelatinosus S1:
RT construction, characterization and complementation of a puf operon deletion
RT strain.";
RL Mol. Gen. Genet. 252:379-385(1996).
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: Cell inner membrane {ECO:0000250}; Multi-pass
CC 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; AY234384; AAB41576.1; -; Genomic_DNA.
DR PIR; S68239; S68239.
DR AlphaFoldDB; P0DJO2; -.
DR SMR; P0DJO2; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
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 GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Bacteriochlorophyll; Cell inner membrane; Cell membrane; Chlorophyll;
KW Chromophore; Electron transport; Herbicide resistance; Iron; Magnesium;
KW Membrane; Metal-binding; Photosynthesis; Reaction center; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..279
FT /note="Reaction center protein L chain"
FT /id="PRO_0000090404"
FT TRANSMEM 33..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..252
FT /note="Helical"
FT /evidence="ECO:0000255"
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 /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT VARIANT 193
FT /note="G -> D (increases resistance to terbutryn 300-fold,
FT slightly increases resistance to atrazine and o-
FT phenanthroline)"
SQ SEQUENCE 279 AA; 31328 MW; 2C15D55FD57913ED CRC64;
MAMLSFEKKY RVRGGTLVGG DLFDFWVGPF YVGFFGVTTL FFSVLGTALI IWGASQGPTW
NLWQISIAPP DLKYGLGVAP LMEGGLWQII TVCAIGAFVS WALREVEICR KLGMQYHVPI
AFSFAILAYV TLVVIRPILM GAWGHGFPYG IFSHLDWVSN VGYQYLHFHY NPAHMLAITF
FFTTTLAMSM HGGLILSAAN PKKGEPMKTT DHEDTFFRDA VGYSIGSLGI HRLGLFLALS
AAFWSAVCIV ISGPFWTRGW PEWWGWWLNL PIWSQWPLN
