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PSBB_OSTTA
ID   PSBB_OSTTA              Reviewed;         454 AA.
AC   Q0P3P8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Photosystem II CP47 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01495};
DE   AltName: Full=PSII 47 kDa protein {ECO:0000255|HAMAP-Rule:MF_01495};
DE   AltName: Full=Protein CP-47 {ECO:0000255|HAMAP-Rule:MF_01495};
GN   Name=psbB {ECO:0000255|HAMAP-Rule:MF_01495}; OrderedLocusNames=OtCpg00040;
OS   Ostreococcus tauri.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595;
RX   PubMed=17251180; DOI=10.1093/molbev/msm012;
RA   Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H., Van de Peer Y.;
RT   "The complete chloroplast and mitochondrial DNA sequence of Ostreococcus
RT   tauri: organelle genomes of the smallest eukaryote are examples of
RT   compaction.";
RL   Mol. Biol. Evol. 24:956-968(2007).
CC   -!- FUNCTION: One of the components of the core complex of photosystem II
CC       (PSII). It binds chlorophyll and helps catalyze the primary light-
CC       induced photochemical processes of PSII. PSII is a light-driven
CC       water:plastoquinone oxidoreductase, using light energy to abstract
CC       electrons from H(2)O, generating O(2) and a proton gradient
CC       subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_01495}.
CC   -!- COFACTOR:
CC       Note=Binds multiple chlorophylls. PSII binds additional chlorophylls,
CC       carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_01495};
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC       PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC       PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC       evolving complex and a large number of cofactors. It forms dimeric
CC       complexes. {ECO:0000255|HAMAP-Rule:MF_01495}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01495}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01495}.
CC   -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01495}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL36329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CR954199; CAL36329.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_717207.1; NC_008289.1.
DR   AlphaFoldDB; Q0P3P8; -.
DR   SMR; Q0P3P8; -.
DR   STRING; 70448.Q0P3P8; -.
DR   PRIDE; Q0P3P8; -.
DR   GeneID; 4238881; -.
DR   KEGG; ota:OstapCp04; -.
DR   eggNOG; ENOG502QRV6; Eukaryota.
DR   InParanoid; Q0P3P8; -.
DR   OrthoDB; 528752at2759; -.
DR   Proteomes; UP000009170; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   HAMAP; MF_01495; PSII_PsbB_CP47; 1.
DR   InterPro; IPR000932; PS_antenna-like.
DR   InterPro; IPR036001; PS_II_antenna-like_sf.
DR   InterPro; IPR017486; PSII_PsbB.
DR   PANTHER; PTHR33180; PTHR33180; 1.
DR   Pfam; PF00421; PSII; 1.
DR   SUPFAM; SSF161077; SSF161077; 1.
DR   TIGRFAMs; TIGR03039; PS_II_CP47; 1.
PE   3: Inferred from homology;
KW   Chlorophyll; Chloroplast; Chromophore; Membrane; Photosynthesis;
KW   Photosystem II; Plastid; Reference proteome; Thylakoid; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..454
FT                   /note="Photosystem II CP47 reaction center protein"
FT                   /id="PRO_0000361021"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        86..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        149..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        183..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        403..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
SQ   SEQUENCE   454 AA;  50028 MW;  FE5393065F360D0C CRC64;
     MWRQGMFVLP FMTRLGVTNS WGGWTISGES TSNPGLWSYE GVAASHIILS GLLFLAAIWH
     WVFWDLELFR DPRTQQPALD LPKIFGIHLF LSGVLCFGFG AFHVTGLFGP GIWVSDPYGL
     TGAVEPVAPA WGAEGFDPYN PGGIAAHHIA AGIVGILAGL FHLSVRPPQR LYKALRMGNV
     ETVLSSSIAA VFWAAFVVGG TMWYGCAATP IELFGPTRYQ WDQGFFQQEI EKRVQTSVAG
     GASLSTAWST IPEKLAFYDY IGNNPAKGGL FRSGPMDNGD GIAAGWLGHA TFTDKNGREL
     FVRRMPTFFE TFPVILIDGD GVVRADVPFR RAESKYSIEQ VGVNVTFYGG ELDGLTFTDP
     ATVKKYARRA QLGEVFEFDR ATLQSDGVFR SSPRAWFTFA HVSFALLFFF GHIWHGARTI
     FRDVFAGIDP DLDEQVEFGA FQKLGDVTTR RQAV
 
 
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