ID   LHA1_RUBGE              Reviewed;          67 AA.
AC   P0DJO0; P51756; P95615;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Light-harvesting protein B-870 alpha chain;
DE   AltName: Full=Antenna pigment protein alpha chain;
DE   AltName: Full=Light-harvesting protein B-875 alpha chain;
GN   Name=pufA;
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=7589500; DOI=10.1016/0014-5793(95)01055-j;
RA   Ouchane S., Picaud M., Astier C.;
RT   "A new mutation in the pufL gene responsible for the terbutryn resistance
RT   phenotype in Rubrivivax gelatinosus.";
RL   FEBS Lett. 374:130-134(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-52, FORMYLATION AT MET-1, AND SUBUNIT STRUCTURE.
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   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the antenna complex alpha subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AY234384; AAO93121.1; -; Genomic_DNA.
DR   PIR; S66179; S66179.
DR   PIR; S66181; S66181.
DR   AlphaFoldDB; P0DJO0; -.
DR   SMR; P0DJO0; -.
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; IPR018332; Antenna_alpha.
DR   InterPro; IPR002361; Antenna_alpha_CS.
DR   InterPro; IPR035889; Light-harvesting_complex.
DR   Pfam; PF00556; LHC; 1.
DR   PRINTS; PR00673; LIGHTHARVSTA.
DR   SUPFAM; SSF56918; SSF56918; 1.
DR   PROSITE; PS00968; ANTENNA_COMP_ALPHA; 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..67
FT                   /note="Light-harvesting protein B-870 alpha chain"
FT                   /id="PRO_0000099792"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..67
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         29
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; in strain DSM 149 and DSM 151"
FT                   /evidence="ECO:0000269|PubMed:8020505"
FT   VARIANT         38
FT                   /note="Y -> F (in strain: DSM 149)"
FT   VARIANT         41
FT                   /note="L -> M (in strain: DSM 151)"
FT   VARIANT         49
FT                   /note="A -> V (in strain: DSM 149)"
FT   VARIANT         51
FT                   /note="T -> S (in strain: DSM 149)"
SQ   SEQUENCE   67 AA;  7348 MW;  12115B467F30135C CRC64;
     MWRIWRLFDP MRAMVAQAVF LLGLAVLIHL MLLGTNKYNW LDGAKKAPAA TAVAPVPAEV
     TSLAQAK