ID   PSBB_ORYSI              Reviewed;         508 AA.
AC   P0C363; P12157; Q6QXT1; Q6QY58;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
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}; ORFNames=9311089;
OS   Oryza sativa subsp. indica (Rice).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND POLYMORPHISM.
RC   STRAIN=cv. 93-11;
RX   PubMed=15122023; DOI=10.1104/pp.103.031245;
RA   Tang J., Xia H., Cao M., Zhang X., Zeng W., Hu S., Tong W., Wang J.,
RA   Wang J., Yu J., Yang H., Zhu L.;
RT   "A comparison of rice chloroplast genomes.";
RL   Plant Physiol. 135:412-420(2004).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY522329; AAS46071.1; -; Genomic_DNA.
DR   RefSeq; YP_654231.1; NC_008155.1.
DR   AlphaFoldDB; P0C363; -.
DR   SMR; P0C363; -.
DR   STRING; 39946.P0C363; -.
DR   PRIDE; P0C363; -.
DR   GeneID; 4126894; -.
DR   Proteomes; UP000007015; 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:0009536; C:plastid; IC:Gramene.
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..508
FT                   /note="Photosystem II CP47 reaction center protein"
FT                   /id="PRO_0000288992"
FT   TRANSMEM        21..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        101..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        140..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        203..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        237..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
FT   TRANSMEM        457..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01495"
SQ   SEQUENCE   508 AA;  56218 MW;  79C9A5853148C0B5 CRC64;
     MGLPWYRVHT VVLNDPGRLL SVHIMHTALV SGWAGSMALY ELAVFDPSDP VLDPMWRQGM
     FVIPFMTRLG ITNSWGGWSI SGGTVTNPGI WSYEGVAGAH IVFSGLCFLA AIWHWVYWDL
     EIFCDERTGK PSLDLPKIFG IHLFLAGVAC FGFGAFHVTG LYGPGIWVSD PYGLTGKVQA
     VNPVWGAEGF DPFVPGGIAS HHIAAGTLGI LAGLFHLSVR PPQRLYKGLR MGNIETVLSS
     SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDQGYF QQEIYRRVSD GLAENLSLSE
     AWSKIPEKLA FYDYIGNNPA KGGLFRAGSM DNGDGIAVGW LGHPIFRDKE GRELFVRRMP
     TFFETFPVVL VDEEGIVRAD VPFRRAESKY SVEQVGVTVE FYGGELNGVS YSDPATVKKY
     ARRSQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHATFAL LFFFGHIWHG ARTLFRDVFA
     GIDPDLDAQV EFGTFQKVGD PTTRRQPV