LHB1_RUBGE
ID LHB1_RUBGE Reviewed; 48 AA.
AC P0DJO1; P51757;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Light-harvesting protein B-870 beta chain;
DE AltName: Full=Antenna pigment protein beta chain;
DE AltName: Full=Light-harvesting protein B-875 beta chain;
GN Name=pufB;
OS Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS gelatinosa).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=28068;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1;
RX PubMed=8879238; DOI=10.1007/bf02173002;
RA Ouchane S., Picaud M., Reiss-Husson F., Vernotte C., Astier C.;
RT "Development of gene transfer methods for Rubrivivax gelatinosus S1:
RT construction, characterization and complementation of a puf operon deletion
RT strain.";
RL Mol. Gen. Genet. 252:379-385(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-48, SUBUNIT STRUCTURE, AND MASS SPECTROMETRY.
RC STRAIN=DSM 149 / LMG 4308 / 2150, and DSM 151 / LMG 4306 / Dr 2;
RX PubMed=8020505; DOI=10.1111/j.1432-1033.1994.tb18911.x;
RA Brunisholz R.A., Suter F., Zuber H.;
RT "Structural and spectral characterisation of the antenna complexes of
RT Rhodocyclus gelatinosus. Indications of a hairpin-like-arranged antenna
RT apoprotein with an unusually high alanine content.";
RL Eur. J. Biochem. 222:667-675(1994).
CC -!- FUNCTION: Antenna complexes are light-harvesting systems, which
CC transfer the excitation energy to the reaction centers.
CC -!- SUBUNIT: An alpha/beta heterodimer. The core complex is formed by
CC different alpha and beta chains, binding bacteriochlorophyll molecules,
CC and arranged most probably in tetrameric structures disposed around the
CC reaction center. The non-pigmented gamma chains may constitute
CC additional components (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane
CC protein.
CC -!- MASS SPECTROMETRY: Mass=5421; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8020505};
CC -!- SIMILARITY: Belongs to the antenna complex beta subunit family.
CC {ECO:0000305}.
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DR EMBL; AY234384; AAO93119.1; -; Genomic_DNA.
DR PIR; B49964; B49964.
DR RefSeq; WP_009857107.1; NZ_SLXD01000003.1.
DR AlphaFoldDB; P0DJO1; -.
DR SMR; P0DJO1; -.
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:8020505"
FT CHAIN 2..48
FT /note="Light-harvesting protein B-870 beta chain"
FT /id="PRO_0000099824"
FT TOPO_DOM 2..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..48
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"
SQ SEQUENCE 48 AA; 5550 MW; 1D077D3269831CD7 CRC64;
MAERKGSISG LTDDEAQEFH KFWVQGFVGF TAVAVVAHFL VWVWRPWL
