RCEL_CERS4
ID RCEL_CERS4 Reviewed; 282 AA.
AC Q3J1A5; P02954; Q9RFB9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Reaction center protein L chain;
DE AltName: Full=Photosynthetic reaction center L subunit;
GN Name=pufL; OrderedLocusNames=RHOS4_18610; ORFNames=RSP_0257;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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). {ECO:0000250}.
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; AF195122; AAF24304.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79429.1; -; Genomic_DNA.
DR PIR; T50760; T50760.
DR RefSeq; WP_002720421.1; NZ_CP030271.1.
DR RefSeq; YP_353330.1; NC_007493.2.
DR PDB; 2WX5; X-ray; 2.63 A; L=2-282.
DR PDB; 4IN5; X-ray; 2.20 A; L=1-282.
DR PDB; 4IN6; X-ray; 2.70 A; L=2-282.
DR PDB; 4N7L; X-ray; 2.85 A; L=2-282.
DR PDB; 5LRI; X-ray; 2.40 A; L=2-282.
DR PDB; 7PIL; EM; 2.50 A; L=2-282.
DR PDBsum; 2WX5; -.
DR PDBsum; 4IN5; -.
DR PDBsum; 4IN6; -.
DR PDBsum; 4N7L; -.
DR PDBsum; 5LRI; -.
DR PDBsum; 7PIL; -.
DR AlphaFoldDB; Q3J1A5; -.
DR SMR; Q3J1A5; -.
DR STRING; 272943.RSP_0257; -.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR EnsemblBacteria; ABA79429; ABA79429; RSP_0257.
DR GeneID; 57470575; -.
DR GeneID; 67446990; -.
DR KEGG; rsp:RSP_0257; -.
DR PATRIC; fig|272943.9.peg.2200; -.
DR eggNOG; ENOG502Z7K3; Bacteria.
DR OMA; WGHGFPY; -.
DR PhylomeDB; Q3J1A5; -.
DR Proteomes; UP000002703; Chromosome 1.
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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..282
FT /note="Reaction center protein L chain"
FT /id="PRO_0000090408"
FT TOPO_DOM 2..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 33..56
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 57..83
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 84..112
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 113..116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..171
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 172..199
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 200..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 226..251
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 252..282
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
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 CONFLICT 55
FT /note="V -> E (in Ref. 1; AAF24304)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="T -> S (in Ref. 1; AAF24304)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="S -> F (in Ref. 1; AAF24304)"
FT /evidence="ECO:0000305"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4IN5"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4IN5"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 33..57
FT /evidence="ECO:0007829|PDB:4IN5"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 85..112
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 172..199
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 227..250
FT /evidence="ECO:0007829|PDB:4IN5"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:4IN5"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:4IN5"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4IN5"
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
