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RCEL_ROSDO
ID   RCEL_ROSDO              Reviewed;         283 AA.
AC   P26280; Q16DV4;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Reaction center protein L chain;
DE   AltName: Full=Photosynthetic reaction center L subunit;
GN   Name=pufL; OrderedLocusNames=RD1_0104;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1787796; DOI=10.1111/j.1365-2958.1991.tb00792.x;
RA   Liebetanz R., Hornberger U., Drews G.;
RT   "Organization of the genes coding for the reaction-centre L and M subunits
RT   and B870 antenna polypeptides alpha and beta from the aerobic
RT   photosynthetic bacterium Erythrobacter species OCH114.";
RL   Mol. Microbiol. 5:1459-1468(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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; X57597; CAA40818.1; -; Genomic_DNA.
DR   EMBL; CP000362; ABG29839.1; -; Genomic_DNA.
DR   RefSeq; WP_011566461.1; NZ_FOOO01000011.1.
DR   AlphaFoldDB; P26280; -.
DR   SMR; P26280; -.
DR   STRING; 375451.RD1_0104; -.
DR   EnsemblBacteria; ABG29839; ABG29839; RD1_0104.
DR   KEGG; rde:RD1_0104; -.
DR   eggNOG; ENOG502Z7K3; Bacteria.
DR   HOGENOM; CLU_078782_0_0_5; -.
DR   OMA; WGHGFPY; -.
DR   OrthoDB; 529504at2; -.
DR   Proteomes; UP000007029; 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   3: Inferred from homology;
KW   Bacteriochlorophyll; Chlorophyll; Chromophore; Electron transport; Iron;
KW   Magnesium; Membrane; Metal-binding; Photosynthesis; Reaction center;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..283
FT                   /note="Reaction center protein L chain"
FT                   /id="PRO_0000090402"
FT   TRANSMEM        33..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        85..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        116..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        171..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        226..252
FT                   /note="Helical"
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   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"
SQ   SEQUENCE   283 AA;  31365 MW;  F83DEB2E50127ADB CRC64;
     MALLSFERKY RVRGGTLVGG DLFDFWVGPF YVGFFGVTTA FFALLGTILI FWGASQQGTF
     NPWLINIAPP DLSYGLGLAP LLEGGLWQII TICATGAFIS WALREVEICR KLGMGYHVPF
     GFAAAIIAYM TLVIFRPLLM GAWGHGFPYG IFSHLDWVSN VGYAYLHFHY NPAHMLAVTL
     FFTTTLALAL HGGLILSACN PEKGEEAKTP DHEDTFFRDF IGYSVGTLGI HRLGYLLAIN
     AGLWSAICII ISGPVWTAGW PEWWNWWLDM PIWGEPIAVI GGM
 
 
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