BCPA_CHLTI
ID BCPA_CHLTI Reviewed; 354 AA.
AC Q46135;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Bacteriochlorophyll a protein;
DE Short=BCP;
DE Short=BChl a protein;
DE AltName: Full=Fenna-Matthews-Olson protein;
DE Short=FMO protein;
DE Flags: Fragment;
GN Name=fmoA;
OS Chlorobaculum thiosulfatiphilum (Chlorobium limicola f.sp.
OS thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=115852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7626630; DOI=10.1021/bi00029a039;
RA Hager-Braun C., Xie D.L., Jarosch U., Herold E., Buttner M., Zimmermann R.,
RA Deutzmann R., Hauska G., Nelson N.;
RT "Stable photobleaching of P840 in Chlorobium reaction center preparations:
RT presence of the 42-kDa bacteriochlorophyll a protein and a 17-kDa
RT polypeptide.";
RL Biochemistry 34:9617-9624(1995).
CC -!- FUNCTION: Intermediary in the transfer of excitation energy from the
CC chlorophyll to the reaction centers.
CC -!- SUBUNIT: Homotrimer. Each subunit contains 7 molecules of
CC bacteriochlorophyll a.
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DR EMBL; X83529; CAA58510.1; -; Genomic_DNA.
DR PIR; S51143; S51143.
DR AlphaFoldDB; Q46135; -.
DR SMR; Q46135; -.
DR PRIDE; Q46135; -.
DR GO; GO:0042314; F:bacteriochlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 2.50.10.10; -; 1.
DR InterPro; IPR003426; BChl_A.
DR InterPro; IPR036559; Chl_A_sf.
DR Pfam; PF02327; BChl_A; 1.
DR SUPFAM; SSF51081; SSF51081; 1.
PE 4: Predicted;
KW Bacteriochlorophyll; Chlorophyll; Chromophore; Electron transport;
KW Magnesium; Metal-binding; Photosynthesis; Reaction center; Transport.
FT CHAIN <1..354
FT /note="Bacteriochlorophyll a protein"
FT /id="PRO_0000064891"
FT BINDING 99
FT /ligand="bacteriochlorophyll a"
FT /ligand_id="ChEBI:CHEBI:61720"
FT /ligand_label="1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="bacteriochlorophyll a"
FT /ligand_id="ChEBI:CHEBI:61720"
FT /ligand_label="6"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="bacteriochlorophyll a"
FT /ligand_id="ChEBI:CHEBI:61720"
FT /ligand_label="4"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="bacteriochlorophyll a"
FT /ligand_id="ChEBI:CHEBI:61720"
FT /ligand_label="7"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="bacteriochlorophyll a"
FT /ligand_id="ChEBI:CHEBI:61720"
FT /ligand_label="3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 354 AA; 39243 MW; F4D4D565BDDCDB1B CRC64;
HRDYEIVLEG GSSSWGKVKA RAKVNVPPAS PLLPADCNVK LNVKPLDPAK GFVRISAVFE
SIVDSTKNKL TIEADIANET KERRISVGEG MVSVGGFSHS FSFEGSVVNM FYYRSDAVRR
NVPNPIYRQG RQFHDILMKV PLDNNDLIDT WEGTVRAIGS TGTFNDWIRD FWFIGPAFTA
LNEGGQRISR IEVNGLNTES GPKGPVGVSR WRFSHGGSGM VDSISRWAEL FPFDKLNRPA
QVEAGFRSDS QGIEVKVDGE FPGVSVDAGG GLRRILNHPL IPLVHHGMVG KFNNFNVDAQ
LKVVLPKGYK VRYAAPQYRS QNLEEYRWSG GAYARWVEHV CKGGVGQFEV LYAQ