ID   LHB1_CERSP              Reviewed;          49 AA.
AC   P0C0Y1; P02951;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Light-harvesting protein B-875 beta chain;
DE   AltName: Full=Antenna pigment protein beta chain;
DE   AltName: Full=LH-3A;
GN   Name=pufB;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-49.
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).
RN   [2]
RP   STRUCTURE BY NMR.
RC   STRAIN=DD13;
RX   PubMed=10756106; DOI=10.1006/jmbi.2000.3649;
RA   Conroy M.J., Westerhuis W.H.J., Parkes-Loach P.S., Loach P.A., Hunter C.N.,
RA   Williamson M.P.;
RT   "The solution structure of Rhodobacter sphaeroides LH1beta reveals two
RT   helical domains separated by a more flexible region: structural
RT   consequences for the LH1 complex.";
RL   J. Mol. Biol. 298:83-94(2000).
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}.
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DR   PIR; B27760; LBRFAS.
DR   PDB; 1DX7; NMR; -; A=2-49.
DR   PDB; 1JO5; NMR; -; A=2-49.
DR   PDBsum; 1DX7; -.
DR   PDBsum; 1JO5; -.
DR   AlphaFoldDB; P0C0Y1; -.
DR   BMRB; P0C0Y1; -.
DR   SMR; P0C0Y1; -.
DR   EvolutionaryTrace; P0C0Y1; -.
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   DisProt; DP01572; -.
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   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   Signal-anchor; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6384009"
FT   CHAIN           2..49
FT                   /note="Light-harvesting protein B-875 beta chain"
FT                   /id="PRO_0000099833"
FT   TOPO_DOM        2..27
FT                   /note="Cytoplasmic"
FT   TRANSMEM        28..45
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        46..49
FT                   /note="Periplasmic"
FT   BINDING         21
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   BINDING         39
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   HELIX           5..8
FT                   /evidence="ECO:0007829|PDB:1DX7"
FT   HELIX           9..20
FT                   /evidence="ECO:0007829|PDB:1DX7"
FT   HELIX           22..31
FT                   /evidence="ECO:0007829|PDB:1DX7"
FT   HELIX           34..44
FT                   /evidence="ECO:0007829|PDB:1DX7"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:1JO5"
SQ   SEQUENCE   49 AA;  5572 MW;  8C5B2F647A157582 CRC64;
     MADKSDLGYT GLTDEQAQEL HSVYMSGLWP FSAVAIVAHL AVYIWRPWF