ID   LHA1_RHOAC              Reviewed;          53 AA.
AC   P35089;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Light-harvesting protein B-800/820 alpha chain;
DE   AltName: Full=Antenna pigment protein alpha chain;
DE   AltName: Full=LH3 complex subunit alpha;
OS   Rhodoblastus acidophilus (Rhodopseudomonas acidophila).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Rhodoblastus.
OX   NCBI_TaxID=1074;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 25092 / 7050 / DSM 137 / LMG 4304 / NCIB 11761;
RA   Brunisholz R.A., Bissig I., Niederer E., Suter F., Zuber H.;
RL   (In) Biggins J. (eds.);
RL   Progress in photosynthesis research, pp.II.1:13-16, Martinus Nijhoff, The
RL   Hague (1987).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-53.
RC   STRAIN=ATCC 25092 / 7050 / DSM 137 / LMG 4304 / NCIB 11761;
RX   PubMed=11467938; DOI=10.1021/bi010309a;
RA   McLuskey K., Prince S.M., Cogdell R.J., Isaacs N.W.;
RT   "The crystallographic structure of the B800-820 LH3 light-harvesting
RT   complex from the purple bacteria Rhodopseudomonas acidophila strain 7050.";
RL   Biochemistry 40:8783-8789(2001).
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   PDB; 1IJD; X-ray; 3.00 A; A/C/E=1-53.
DR   PDBsum; 1IJD; -.
DR   AlphaFoldDB; P35089; -.
DR   SMR; P35089; -.
DR   DrugBank; DB04464; N-Formylmethionine.
DR   EvolutionaryTrace; P35089; -.
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   3D-structure; Antenna complex; Bacteriochlorophyll; Cell inner membrane;
KW   Cell membrane; Chlorophyll; Chromophore; Direct protein sequencing;
KW   Light-harvesting polypeptide; Magnesium; Membrane; Metal-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..53
FT                   /note="Light-harvesting protein B-800/820 alpha chain"
FT                   /id="PRO_0000099784"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..53
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         31
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"
FT   HELIX           4..8
FT                   /evidence="ECO:0007829|PDB:1IJD"
FT   HELIX           12..36
FT                   /evidence="ECO:0007829|PDB:1IJD"
FT   HELIX           40..44
FT                   /evidence="ECO:0007829|PDB:1IJD"
SQ   SEQUENCE   53 AA;  5546 MW;  46CD3C558C8B0A60 CRC64;
     MNQGKIWTVV PPAFGLPLML GAVAITALLV HAAVLTHTTW YAAFLQGGVK KAA