ID   RCEL_ACICY              Reviewed;         252 AA.
AC   O66137;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Reaction center protein L chain;
DE   AltName: Full=Photosynthetic reaction center L subunit;
DE   Flags: Fragment;
GN   Name=pufL;
OS   Acidiphilium cryptum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=524;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9435141; DOI=10.1093/oxfordjournals.pcp.a029112;
RA   Nagashima K.V., Matsuura K., Wakao N., Hiraishi A., Shimada K.;
RT   "Nucleotide sequences of genes coding for photosynthetic reaction centers
RT   and light-harvesting proteins of Acidiphilium rubrum and related aerobic
RT   acidophilic bacteria.";
RL   Plant Cell Physiol. 38:1249-1258(1997).
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 two highly
CC       hydrophobic polypeptide chains (designated L and M).
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; AB005220; BAA25561.1; -; Genomic_DNA.
DR   AlphaFoldDB; O66137; -.
DR   SMR; O66137; -.
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   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; Iron; Magnesium; Membrane; Metal-binding;
KW   Photosynthesis; Reaction center; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           <1..252
FT                   /note="Reaction center protein L chain"
FT                   /id="PRO_0000090397"
FT   TRANSMEM        8..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         128
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         148
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         165
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   252 AA;  27456 MW;  3ED0C38CFB1069EF CRC64;
     VGPFYVGFFG VTAAFFIMLG TALIIWGAAL GPTWNIWQIS IAPPDLSYGL GLAPLAKGGL
     WQIITVCAIG AFGSWALREV EISRKLGIGL HVPAAFSVAI FAYVTLEVIR PLLMGAWGNG
     FPYGIMSHLD WVSNTGYAYL NFEYNPMHMV AVTLFFTTTL ALALHGSLVL AAINPPAGET
     VKFAEHEDTF FRDFIGYSIG TLGIHRLGLF LALGAGFASA TCILLSGPFW TQGWPSWWGW
     WLHLPIWQFG GH