ID   LHB2_RHOCA              Reviewed;          49 AA.
AC   P07368;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   03-AUG-2022, entry version 111.
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   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16593533; DOI=10.1073/pnas.82.1.58;
RA   Youvan D.C., Ismail S.;
RT   "Light-harvesting II (B800-B850 complex) structural genes from
RT   Rhodopseudomonas capsulata.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:58-62(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2549005; DOI=10.1128/jb.171.9.4914-4922.1989;
RA   Tichy H.V., Oberle B., Stiehle H., Schiltz E., Drews G.;
RT   "Genes downstream from pucB and pucA are essential for formation of the
RT   B800-850 complex of Rhodobacter capsulatus.";
RL   J. Bacteriol. 171:4914-4922(1989).
RN   [3]
RP   PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
RX   DOI=10.1016/0014-5793(85)80960-1;
RA   Tadros M.H., Frank R., Drews G.;
RT   "The complete amino-acid sequence of the small bacteriochlorophyll-binding
RT   polypeptide B800-850-beta from light-harvesting complex B800-850 of
RT   Rhodopseudomonas capsulata.";
RL   FEBS Lett. 183:91-94(1985).
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; K02337; AAA26132.1; -; Genomic_DNA.
DR   EMBL; M28510; AAA26161.1; -; Genomic_DNA.
DR   PIR; A21901; LBRF8C.
DR   RefSeq; WP_013068239.1; NZ_VIBE01000014.1.
DR   AlphaFoldDB; P07368; -.
DR   SMR; P07368; -.
DR   GeneID; 31491357; -.
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; Formylation;
KW   Light-harvesting polypeptide; Magnesium; Membrane; Metal-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..49
FT                   /note="Light-harvesting protein B-800/850 beta chain"
FT                   /id="PRO_0000099823"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        22..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..49
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         20
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         38
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; partial"
FT                   /evidence="ECO:0000269|Ref.3"
SQ   SEQUENCE   49 AA;  5155 MW;  6CDDDE07B396211B CRC64;
     MTDDKAGPSG LSLKEAEEIH SYLIDGTRVF GAMALVAHIL SAIATPWLG