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RCEL_RHOCA
ID   RCEL_RHOCA              Reviewed;         282 AA.
AC   P19057;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Reaction center protein L chain;
DE   AltName: Full=Photosynthetic reaction center L subunit;
GN   Name=pufL;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6744416; DOI=10.1016/0092-8674(84)90429-x;
RA   Youvan D.C., Bylina E.J., Alberti M., Begusch H., Hearst J.E.;
RT   "Nucleotide and deduced polypeptide sequences of the photosynthetic
RT   reaction-center, B870 antenna, and flanking polypeptides from R.
RT   capsulata.";
RL   Cell 37:949-957(1984).
RN   [2]
RP   3D-STRUCTURE MODELING.
RX   PubMed=7479696; DOI=10.1002/prot.340220304;
RA   Foloppe N., Ferrand M., Breton J., Smith J.C.;
RT   "Structural model of the photosynthetic reaction center of Rhodobacter
RT   capsulatus.";
RL   Proteins 22:226-244(1995).
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; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC       {ECO:0000305}.
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DR   EMBL; K01184; AAA26174.1; -; Genomic_DNA.
DR   EMBL; K01183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z11165; CAA77554.1; -; Genomic_DNA.
DR   PIR; B28771; B28771.
DR   RefSeq; WP_013066437.1; NZ_VIBE01000010.1.
DR   AlphaFoldDB; P19057; -.
DR   SMR; P19057; -.
DR   GeneID; 31489639; -.
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   3: Inferred from homology;
KW   Bacteriochlorophyll; Chlorophyll; Chromophore; Electron transport; Iron;
KW   Magnesium; Membrane; Metal-binding; Photosynthesis; Reaction center;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..282
FT                   /note="Reaction center protein L chain"
FT                   /id="PRO_0000090403"
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                   /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   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"
SQ   SEQUENCE   282 AA;  31567 MW;  066A9D58A7900460 CRC64;
     MALLSFERKY RVPGGTLIGG SLFDFWVGPF YVGFFGVTTI FFATLGFLLI LWGAAMQGTW
     NPQLISIFPP PVENGLNVAA LDKGGLWQVI TVCATGAFCS WALREVEICR KLGIGFHIPV
     AFSMAIFAYL TLVVIRPMMM GSWGYAFPYG IWTHLDWVSN TGYTYGNFHY NPFHMLGISL
     FFTTAWALAM HGALVLSAAN PVKGKTMRTP DHEDTYFRDL MGYSVGTLGI HRLGLLLALN
     AVFWSACCML VSGTIYFDLW SDWWYWWVNM PFWADMAGGI NG
 
 
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