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 13-SEP-2023, entry version 72. 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; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; 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}. 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; 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: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 NCBIfam; NF040862; pufB_517_ASD; 1. DR Pfam; PF00556; LHC; 1. DR PIRSF; PIRSF002900; Antenna_beta; 1. DR PRINTS; PR00674; LIGHTHARVSTB. DR SUPFAM; SSF56918; Light-harvesting complex subunits; 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 //