BCPA_PROAE
ID BCPA_PROAE Reviewed; 366 AA.
AC P11741;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Bacteriochlorophyll a protein;
DE Short=BCP;
DE Short=BChl a protein;
OS Prosthecochloris aestuarii.
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=1102;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=2K;
RX PubMed=3949780; DOI=10.1016/s0021-9258(17)35690-9;
RA Daurat-Larroque S.T., Brew K., Fenna R.E.;
RT "The complete amino acid sequence of a bacteriochlorophyll a-protein from
RT Prosthecochloris aestuarii.";
RL J. Biol. Chem. 261:3607-3615(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3735428; DOI=10.1016/0022-2836(86)90167-1;
RA Tronrud D.E., Schmid M.F., Matthews B.W.;
RT "Structure and X-ray amino acid sequence of a bacteriochlorophyll a protein
RT from Prosthecochloris aestuarii refined at 1.9-A resolution.";
RL J. Mol. Biol. 188:443-454(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=490647; DOI=10.1016/0022-2836(79)90076-7;
RA Matthews B.W., Fenna R.E., Bolognesi M.C., Schmid M.F., Olson J.M.;
RT "Structure of a bacteriochlorophyll a-protein from the green photosynthetic
RT bacterium Prosthecochloris aestuarii.";
RL J. Mol. Biol. 131:259-285(1979).
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A25002; A25002.
DR PIR; A25330; A25330.
DR PDB; 3EOJ; X-ray; 1.30 A; A=1-366.
DR PDB; 4BCL; X-ray; 1.90 A; A=1-366.
DR PDB; 6MEZ; X-ray; 1.74 A; A/B=7-366.
DR PDBsum; 3EOJ; -.
DR PDBsum; 4BCL; -.
DR PDBsum; 6MEZ; -.
DR AlphaFoldDB; P11741; -.
DR SMR; P11741; -.
DR DrugBank; DB01853; Bacteriochlorophyll A.
DR PRIDE; P11741; -.
DR EvolutionaryTrace; P11741; -.
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 1: Evidence at protein level;
KW 3D-structure; Bacteriochlorophyll; Chlorophyll; Chromophore;
KW Direct protein sequencing; Electron transport; Magnesium; Metal-binding;
KW Photosynthesis; Reaction center; Transport.
FT CHAIN 1..366
FT /note="Bacteriochlorophyll a protein"
FT /id="PRO_0000064893"
FT BINDING 110
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 BINDING 145
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 BINDING 290
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 BINDING 297
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 BINDING 298
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 STRAND 10..19
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 42..56
FT /evidence="ECO:0007829|PDB:3EOJ"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:6MEZ"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 77..105
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 108..124
FT /evidence="ECO:0007829|PDB:3EOJ"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:3EOJ"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:3EOJ"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:3EOJ"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3EOJ"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 218..231
FT /evidence="ECO:0007829|PDB:3EOJ"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:3EOJ"
FT TURN 238..242
FT /evidence="ECO:0007829|PDB:3EOJ"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:3EOJ"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:3EOJ"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:3EOJ"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:3EOJ"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:3EOJ"
SQ SEQUENCE 366 AA; 40276 MW; 57242734E53615B1 CRC64;
ALFGTKDTTT AHSDYEIILE GGSSSWGQVK GRAKVNVPAA IPLLPTDCNI RIDAKPLDAQ
KGVVRFTTKI ESVVDSVKNT LNVEVDIANE TKDRRIAVGE GSLSVGDFSH SFSFEGQVVN
MYYYRSDAVR RNIPNPIYMQ GRQFHDILMK VPLDNNDLVD TWEGFQQSIS GGGANFGDWI
REFWFIGPAF AAINEGGQRI SPIVVNSSNV EGGEKGPVGV TRWKFSHAGS GVVDSISRWT
ELFPVEQLNK PASIEGGFRS DSQGIEVKVD GNLPGVSRDA GGGLRRILNH PLIPLVHHGM
VGKFNDFTVD TQLKIVLPKG YKIRYAAPQF RSQNLEEYRW SGGAYARWVE HVCKGGTGQF
EVLYAQ
