ID   LHB2_HALHL              Reviewed;          51 AA.
AC   P80105;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Light-harvesting protein B800/850/890 beta-2 chain;
DE   AltName: Full=Antenna pigment protein beta-2 chain;
DE   AltName: Full=EHA-beta-2;
DE   Flags: Fragment;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1577009; DOI=10.1111/j.1432-1033.1992.tb16858.x;
RA   Wagner-Huber R., Brunisholz R.A., Bissig I., Frank G., Suter F., Zuber H.;
RT   "The primary structure of the antenna polypeptides of Ectothiorhodospira
RT   halochloris and Ectothiorhodospira halophila. Four core-type antenna
RT   polypeptides in E. halochloris and E. halophila.";
RL   Eur. J. Biochem. 205:917-925(1992).
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; S23291; S23291.
DR   AlphaFoldDB; P80105; -.
DR   SMR; P80105; -.
DR   STRING; 349124.Hhal_1607; -.
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..>51
FT                   /note="Light-harvesting protein B800/850/890 beta-2 chain"
FT                   /id="PRO_0000099811"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..>51
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         16
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         34
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   NON_TER         51
SQ   SEQUENCE   51 AA;  5739 MW;  281399601520AFCE CRC64;
     ADEMRNVSDE EAKEFHAMFS QAFTVYVGVA VVAHILAWAW RPWIPGDEGF G