ID   LHA1_CERSP              Reviewed;          58 AA.
AC   P0C0X9; P02949;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Light-harvesting protein B-875 alpha chain;
DE   AltName: Full=Antenna pigment protein alpha chain;
DE   AltName: Full=LH-1;
GN   Name=pufA;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
RC   STRAIN=R-26.1;
RX   PubMed=6384009; DOI=10.1515/bchm2.1984.365.2.703;
RA   Theiler R., Suter F., Wiemken V., Zuber H.;
RT   "The light-harvesting polypeptides of Rhodopseudomonas sphaeroides R-26.1.
RT   I. Isolation, purification and sequence analyses.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 365:703-719(1984).
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   PIR; A27760; LBRF1S.
DR   RefSeq; WP_002720422.1; NZ_WTFI01000017.1.
DR   PDB; 4V9G; X-ray; 7.78 A; A1/A2/A3/A5/A7/AD/AF/AJ/AN/AP/AT/AV/AX/AZ/B1/B2/B3/B5/B7/BD/BF/BJ/BN/BP/BT/BV/BX/BZ=1-58.
DR   PDB; 7F0L; EM; 2.94 A; 5/7=1-54.
DR   PDBsum; 4V9G; -.
DR   PDBsum; 7F0L; -.
DR   AlphaFoldDB; P0C0X9; -.
DR   SMR; P0C0X9; -.
DR   GeneID; 57470576; -.
DR   GeneID; 67446991; -.
DR   OMA; NWLEGPR; -.
DR   OrthoDB; 2077221at2; -.
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   Formylation; Light-harvesting polypeptide; Magnesium; Membrane;
KW   Metal-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..58
FT                   /note="Light-harvesting protein B-875 alpha chain"
FT                   /id="PRO_0000099801"
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"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:6384009"
FT   HELIX           4..9
FT                   /evidence="ECO:0007829|PDB:7F0L"
FT   HELIX           13..37
FT                   /evidence="ECO:0007829|PDB:7F0L"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:7F0L"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:7F0L"
SQ   SEQUENCE   58 AA;  6809 MW;  ACCB5E84354A9117 CRC64;
     MSKFYKIWMI FDPRRVFVAQ GVFLFLLAVM IHLILLSTPS YNWLEISAAK YNRVAVAE