LHA_ROSDO
ID LHA_ROSDO Reviewed; 52 AA.
AC P26273; Q16DV2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Light-harvesting protein B-870 alpha chain;
DE AltName: Full=Antenna pigment protein alpha chain;
GN Name=pufA; OrderedLocusNames=RD1_0106;
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1787796; DOI=10.1111/j.1365-2958.1991.tb00792.x;
RA Liebetanz R., Hornberger U., Drews G.;
RT "Organization of the genes coding for the reaction-centre L and M subunits
RT and B870 antenna polypeptides alpha and beta from the aerobic
RT photosynthetic bacterium Erythrobacter species OCH114.";
RL Mol. Microbiol. 5:1459-1468(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114;
RX PubMed=17098896; DOI=10.1128/jb.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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 alpha subunit family.
CC {ECO:0000305}.
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DR EMBL; X57597; CAA40817.1; -; Genomic_DNA.
DR EMBL; CP000362; ABG29841.1; -; Genomic_DNA.
DR RefSeq; WP_011566463.1; NZ_FOOO01000011.1.
DR AlphaFoldDB; P26273; -.
DR SMR; P26273; -.
DR STRING; 375451.RD1_0106; -.
DR EnsemblBacteria; ABG29841; ABG29841; RD1_0106.
DR KEGG; rde:RD1_0106; -.
DR eggNOG; ENOG5032QBE; Bacteria.
DR HOGENOM; CLU_205201_0_0_5; -.
DR OMA; WFENAAM; -.
DR OrthoDB; 2077221at2; -.
DR Proteomes; UP000007029; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
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; 4.10.220.20; -; 1.
DR InterPro; IPR000066; Antenna_a/b.
DR InterPro; IPR002361; Antenna_alpha_CS.
DR InterPro; IPR035889; Light-harvesting_complex.
DR Pfam; PF00556; LHC; 1.
DR SUPFAM; SSF56918; SSF56918; 1.
DR PROSITE; PS00968; ANTENNA_COMP_ALPHA; 1.
PE 3: Inferred from homology;
KW Antenna complex; Bacteriochlorophyll; Cell inner membrane; Cell membrane;
KW Chlorophyll; Chromophore; Light-harvesting polypeptide; Magnesium;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..52
FT /note="Light-harvesting protein B-870 alpha chain"
FT /id="PRO_0000099783"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..52
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 32
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 52 AA; 5814 MW; DD9B650B2F3B45B0 CRC64;
MAKFYKIWLI FDPRRVFVAQ GVFLFLLAAM IHLVVLSSGL NWFEAAAAVG GQ