RCEL_RHOPA
ID RCEL_RHOPA Reviewed; 277 AA.
AC O83005;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Reaction center protein L chain;
DE AltName: Full=Photosynthetic reaction center L subunit;
GN Name=pufL; OrderedLocusNames=RPA1527;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HMD002;
RA Hamada T.;
RT "Use of gyrB gene, pufL and pufM genes and 16S rRNA sequence analysis to
RT investigate phylogeny of photosynthetic bacteria.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; AB015977; BAA33001.1; -; mRNA.
DR EMBL; BX572597; CAE26969.1; -; Genomic_DNA.
DR RefSeq; WP_011157088.1; NC_005296.1.
DR PDB; 6Z5R; EM; 2.80 A; L=1-277.
DR PDB; 6Z5S; EM; 2.65 A; L=1-277.
DR PDBsum; 6Z5R; -.
DR PDBsum; 6Z5S; -.
DR AlphaFoldDB; O83005; -.
DR SMR; O83005; -.
DR STRING; 258594.RPA1527; -.
DR PRIDE; O83005; -.
DR EnsemblBacteria; CAE26969; CAE26969; RPA1527.
DR GeneID; 66892558; -.
DR KEGG; rpa:RPA1527; -.
DR eggNOG; ENOG502Z7K3; Bacteria.
DR HOGENOM; CLU_078782_0_0_5; -.
DR OMA; WGHGFPY; -.
DR PhylomeDB; O83005; -.
DR BioCyc; RPAL258594:TX73_RS07790-MON; -.
DR Proteomes; UP000001426; Chromosome.
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..277
FT /note="Reaction center protein L chain"
FT /id="PRO_0000090405"
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..255
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 CONFLICT 34
FT /note="I -> F (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..39
FT /note="MT -> TA (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="F -> C (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 45..47
FT /note="IGI -> MGT (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="A -> I (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..93
FT /note="SIC -> TIF (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 99..100
FT /note="VT -> CS (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="F -> Y (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="V -> L (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="S -> Q (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="Y -> W (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="A -> G (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="L -> I (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="L -> V (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="F -> W (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="I -> L (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="A -> P (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="D -> E (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="N -> E (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT CONFLICT 271..272
FT /note="NL -> RI (in Ref. 1; BAA33001)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6Z5S"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 33..56
FT /evidence="ECO:0007829|PDB:6Z5S"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 85..112
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 172..199
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 226..250
FT /evidence="ECO:0007829|PDB:6Z5S"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:6Z5S"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6Z5S"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6Z5S"
SQ SEQUENCE 277 AA; 30837 MW; 956B6710FC595013 CRC64;
MAMLSFEKKY RVRGGTLIGG DLFDFWVGPF YVGIFGVMTV FFALIGIALI AWNTALGPTW
NLWQISVNPP DAKYGLGFAP LAEGGIWQWV SICATGAFVT WALREVEICR KLGIGFHVPF
AFSFAIFAYV TLVVIRPVLM GSWSYGFPYG IFTHLDWVSN TGYSYGQFHY NPAHMIAITF
FFTTCLALAL HGGLVLSALN PDRGEPVKSP EHENTVFRDL VGYSIGTIGI HRLGLFLALS
AVFFSAVCMI ISGPVLAEGG SWPDWWNWWR NLPIWNP
