ID   LHB2_RHOSU              Reviewed;          51 AA.
AC   P95654;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Light-harvesting protein B-800/850 beta chain;
DE   AltName: Full=Antenna pigment protein beta chain;
DE   AltName: Full=LH-3B;
GN   Name=pucB;
OS   Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodovulum.
OX   NCBI_TaxID=35806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W4;
RX   PubMed=9130598; DOI=10.1016/s0167-4781(96)00228-x;
RA   Hagemann G.E., Katsiou E., Forkl H., Steindorf A.C., Tadros M.H.;
RT   "Gene cloning and regulation of gene expression of the puc operon from
RT   Rhodovulum sulfidophilum.";
RL   Biochim. Biophys. Acta 1351:341-358(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-51.
RC   STRAIN=W4;
RX   PubMed=7628614; DOI=10.1016/0014-5793(95)00645-p;
RA   Tadros M.H., Hagemann G.E., Katsiou E., Dierstein R., Schiltz E.;
RT   "Isolation and complete amino acid sequence of the beta- and alpha-
RT   polypeptides from the peripheral light-harvesting pigment-protein complex
RT   II of Rhodobacter sulfidophilus.";
RL   FEBS Lett. 368:243-247(1995).
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   EMBL; U81968; AAB59006.1; -; Genomic_DNA.
DR   PIR; S66224; S66224.
DR   RefSeq; WP_042460741.1; NZ_MSYR01000001.1.
DR   AlphaFoldDB; P95654; -.
DR   SMR; P95654; -.
DR   STRING; 1188256.BASI01000002_gene3402; -.
DR   GeneID; 62371207; -.
DR   eggNOG; ENOG50331U4; Bacteria.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7628614"
FT   CHAIN           2..51
FT                   /note="Light-harvesting protein B-800/850 beta chain"
FT                   /id="PRO_0000099837"
FT   TOPO_DOM        2..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..51
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         22
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   BINDING         40
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   51 AA;  5569 MW;  A96F52CCFBD74661 CRC64;
     MTDDMDKVWP TGLTLAEAEE VHKQLIDGTR VFGAIALFAH FLAAIATPWL G