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LHA2_RHOCA
ID   LHA2_RHOCA              Reviewed;          60 AA.
AC   P07367;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Light-harvesting protein B-800/850 alpha chain;
DE   AltName: Full=Antenna pigment protein alpha chain;
DE   AltName: Full=LH-2;
GN   Name=pucA;
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.
RX   PubMed=6825670; DOI=10.1111/j.1432-1033.1983.tb07081.x;
RA   Tadros M.H., Suter F., Drews G., Zuber H.;
RT   "The complete amino-acid sequence of the large bacteriochlorophyll-binding
RT   polypeptide from light-harvesting complex II (B800-850) of Rhodopseudomonas
RT   capsulata.";
RL   Eur. J. Biochem. 129:533-536(1983).
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; K02337; AAA26133.1; -; Genomic_DNA.
DR   EMBL; M28510; AAA26162.1; -; Genomic_DNA.
DR   PIR; B21901; LBRFA8.
DR   RefSeq; WP_013068240.1; NZ_VIBE01000014.1.
DR   AlphaFoldDB; P07367; -.
DR   SMR; P07367; -.
DR   GeneID; 31491358; -.
DR   OMA; SHTTWFP; -.
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;
KW   Light-harvesting polypeptide; Magnesium; Membrane; Metal-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..60
FT                   /note="Light-harvesting protein B-800/850 alpha chain"
FT                   /id="PRO_0000099791"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..60
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         31
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   60 AA;  6259 MW;  A5709A614C18B6A6 CRC64;
     MNNAKIWTVV KPSTGIPLIL GAVAVAALIV HAGLLTNTTW FANYWNGNPM ATVVAVAPAQ
 
 
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