ID   PSBB_OENAR              Reviewed;         508 AA.
AC   P19819; B0Z4Q2;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 94.
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};
OS   Oenothera argillicola (Appalachian evening primrose).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX   NCBI_TaxID=3940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2243806; DOI=10.1093/nar/18.21.6452;
RA   Offermann-Steinhard K., Herrmann R.G.;
RT   "Nucleotide sequences of psbB and psbH, the plastid encoded genes for CP47
RT   and the 10 kDa phosphoprotein of photosystem II in Oenothera hookeri and
RT   argillicola.";
RL   Nucleic Acids Res. 18:6452-6452(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Douthat 1;
RX   PubMed=18299283; DOI=10.1093/nar/gkn081;
RA   Greiner S., Wang X., Rauwolf U., Silber M.V., Mayer K., Meurer J.,
RA   Haberer G., Herrmann R.G.;
RT   "The complete nucleotide sequences of the five genetically distinct plastid
RT   genomes of Oenothera, subsection Oenothera: I. Sequence evaluation and
RT   plastome evolution.";
RL   Nucleic Acids Res. 36:2366-2378(2008).
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}.
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DR   EMBL; X55899; CAA39388.1; -; Genomic_DNA.
DR   EMBL; EU262887; ABW98730.1; -; Genomic_DNA.
DR   PIR; S12129; S12129.
DR   RefSeq; YP_001687163.1; NC_010358.2.
DR   AlphaFoldDB; P19819; -.
DR   SMR; P19819; -.
DR   GeneID; 5951870; -.
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; Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..508
FT                   /note="Photosystem II CP47 reaction center protein"
FT                   /id="PRO_0000077490"
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;  55998 MW;  BADD8FEBAAC802BF CRC64;
     MGLPWYRVHT VVLNDPGRLL AVHIMHTALV AGWAGSMALY ELAVFDPSDP VLDPMWRQGM
     FVIPFMTRLG ITNSWGGWSI TGGTVTNPGI WSYEGVAGSH ILFSGLCFLA AIWHWVYWDL
     AIFSDERTGK PSLDLPKIFG IHLFLSGLAC FGFGAFHVTG LYGPGIWVSD PYGLTGEVQP
     VNPAWGVEGF DPFVPGGIAS HHIAAGTLGI LAGLFHLSVR PPQRLYKGLR MGNIETVLSS
     SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDQGYF QQEIYRRVGA GLAKNQSLSE
     AWSKIPEKLA FYDYIGNNPA KGGLFRAGSM DSGDGIAVGW LGHPIFRDKE GRELFVRRMP
     TFFETFPVVL VDGDGIVRAD VPFRRAESKY SVEQVGVTVE FYGGELNGVS YSDPATVKKY
     ARRAQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHASFAL LFFFGHIWHG ARTLFRDVFA
     GIDPDLDTQV EFGAFQKLGD PTTRRQAV