ID   LHB1_RHOTE              Reviewed;          48 AA.
AC   P80590;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Light-harvesting polypeptide B-885 beta-1 chain;
DE            Short=LH-1;
DE   AltName: Full=Antenna pigment polypeptide beta-1 chain;
OS   Rhodocyclus tenuis (Rhodospirillum tenue).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Rhodocyclus.
OX   NCBI_TaxID=1066;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 25093 / DSM 109 / 2761;
RX   PubMed=8681949; DOI=10.1111/j.1432-1033.1996.0381z.x;
RA   Hu Q., Brunisholz R.A., Frank G., Zuber H.;
RT   "The antenna complexes of the purple non-sulfur photosynthetic bacterium
RT   Rhodocyclus tenuis. Structural and spectral characterization.";
RL   Eur. J. Biochem. 238:381-390(1996).
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 beta subunit family.
CC       {ECO:0000305}.
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; S68885; S68885.
DR   AlphaFoldDB; P80590; -.
DR   SMR; P80590; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 1.20.5.250; -; 1.
DR   InterPro; IPR000066; Antenna_a/b.
DR   InterPro; IPR023623; Antenna_beta_CS.
DR   InterPro; IPR023624; Antenna_beta_dom_sf.
DR   InterPro; IPR002362; LHB-1/5.
DR   InterPro; IPR035889; Light-harvesting_complex.
DR   Pfam; PF00556; LHC; 1.
DR   PIRSF; PIRSF002900; Antenna_beta; 1.
DR   PRINTS; PR00674; LIGHTHARVSTB.
DR   SUPFAM; SSF56918; SSF56918; 1.
DR   PROSITE; PS00969; ANTENNA_COMP_BETA; 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..48
FT                   /note="Light-harvesting polypeptide B-885 beta-1 chain"
FT                   /id="PRO_0000099839"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..48
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         37
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   48 AA;  5344 MW;  8CB2F1C3736F0086 CRC64;
     AEDRKSLSGL TEQEAQEFGT LYTQGVAFVA VIAVVAHALV WAWRPWLQ