LHA1_RHOCA
ID LHA1_RHOCA Reviewed; 58 AA.
AC P02948;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Light-harvesting protein B-870 alpha chain;
DE AltName: Full=Antenna pigment protein alpha chain;
DE AltName: Full=LH-1;
GN Name=pufA;
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=16593406; DOI=10.1073/pnas.81.1.189;
RA Youvan D.C., Alberti M., Begusch H., Bylina E.J., Hearst J.E.;
RT "Reaction center and light-harvesting I genes from Rhodopseudomonas
RT capsulata.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:189-192(1984).
RN [2]
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 [3]
RP PROTEIN SEQUENCE.
RA Tadros M.H., Frank G., Zuber H., Drews G.;
RT "The complete amino acid sequence of the large bacteriochlorophyll-binding
RT polypeptide B870-alpha from the light-harvesting complex B870 of
RT Rhodopseudomonas capsulata.";
RL FEBS Lett. 190:41-44(1985).
CC -!- FUNCTION: Antenna complexes are light-harvesting systems, which
CC transfer the excitation energy to the reaction centers.
CC -!- SUBUNIT: The core complex is formed by different alpha and beta chains,
CC binding bacteriochlorophyll molecules, and arranged most probably in
CC tetrameric structures disposed around the reaction center. The non-
CC pigmented gamma chains may constitute additional components.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane
CC protein.
CC -!- SIMILARITY: Belongs to the antenna complex alpha subunit family.
CC {ECO:0000305}.
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DR EMBL; K01184; AAA26173.1; -; Genomic_DNA.
DR EMBL; Z11165; CAA77553.1; -; Genomic_DNA.
DR PIR; A03449; LBRFAC.
DR RefSeq; WP_013066436.1; NZ_VIBE01000010.1.
DR AlphaFoldDB; P02948; -.
DR SMR; P02948; -.
DR GeneID; 31489638; -.
DR OMA; NWLEGPR; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
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:0019684; P:photosynthesis, light reaction; IEA:InterPro.
DR Gene3D; 4.10.220.20; -; 1.
DR InterPro; IPR000066; Antenna_a/b.
DR InterPro; IPR018332; Antenna_alpha.
DR InterPro; IPR002361; Antenna_alpha_CS.
DR InterPro; IPR035889; Light-harvesting_complex.
DR Pfam; PF00556; LHC; 1.
DR PRINTS; PR00673; LIGHTHARVSTA.
DR SUPFAM; SSF56918; SSF56918; 1.
DR PROSITE; PS00968; ANTENNA_COMP_ALPHA; 1.
PE 1: Evidence at protein level;
KW Antenna complex; Bacteriochlorophyll; Cell inner membrane; Cell membrane;
KW Chlorophyll; Chromophore; Direct protein sequencing;
KW Light-harvesting polypeptide; Magnesium; Membrane; Metal-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..58
FT /note="Light-harvesting protein B-870 alpha chain"
FT /id="PRO_0000099790"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..58
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 32
FT /ligand="a bacteriochlorophyll"
FT /ligand_id="ChEBI:CHEBI:38201"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
SQ SEQUENCE 58 AA; 6594 MW; 53178828AA93C93D CRC64;
MSKFYKIWLV FDPRRVFVAQ GVFLFLLAVL IHLILLSTPA FNWLTVATAK HGYVAAAQ