ID   PSBB_WELMI              Reviewed;         508 AA.
AC   B2Y1Y5; B7ZI23;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 41.
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   Welwitschia mirabilis (Tree tumbo) (Welwitschia bainesii).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Gnetopsida; Gnetidae; Welwitschiales; Welwitschiaceae;
OC   Welwitschia.
OX   NCBI_TaxID=3377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18452621; DOI=10.1186/1471-2148-8-130;
RA   McCoy S.R., Kuehl J.V., Boore J.L., Raubeson L.A.;
RT   "The complete plastid genome sequence of Welwitschia mirabilis: an
RT   unusually compact plastome with accelerated divergence rates.";
RL   BMC Evol. Biol. 8:130-130(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19166950; DOI=10.1016/j.ympev.2008.12.026;
RA   Wu C.-S., Lai Y.-T., Lin C.-P., Wang Y.-N., Chaw S.-M.;
RT   "Evolution of reduced and compact chloroplast genomes (cpDNAs) in
RT   gnetophytes: Selection toward a lower-cost strategy.";
RL   Mol. Phylogenet. Evol. 52:115-124(2009).
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; EU342371; ABY26815.1; -; Genomic_DNA.
DR   EMBL; AP009568; BAH11203.1; -; Genomic_DNA.
DR   RefSeq; YP_001876602.1; NC_010654.1.
DR   AlphaFoldDB; B2Y1Y5; -.
DR   SMR; B2Y1Y5; -.
DR   GeneID; 6276237; -.
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_0000359867"
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;  56163 MW;  C623E4F704BDF598 CRC64;
     MGLPWYRVHT VVLNDPGRLI AVHIMHTALV AGWAGSMALY ELAVFDPSDS VLDPMWRQGM
     FILPFMTRLG IKESWGGWSI TGEPIANPGL WSYEGVAGAH IVFSGLCFLS ATWHWVYWDL
     EIFSDPRTGK PSLDLPKIFG IHLFLSGVAC FGFGAFHVTG LYGPGIWVSD PFGLTGKIQP
     VSPAWGAEGF DPFVPGGIAS HHVAAGLLGI IAGLFHLSVR PPQRLYRGLR MGNIETVLSS
     SIAAVFFAAF IVAGTMWYGS ATTPIELFGP TRYQWDQGYF QQEIDRRVQA GLAENLSLSE
     AWSRIPEKLA FYDYIGNNPA KGGLFRAGAM DNGDGIAVGW LGHPIFKDKE GNELFVRRMP
     TFFETFPVVL VDKEGVIKAD IPFRRAESKY SVEQVGVTVE FYGGELNGVS FSDPAIVKKY
     ARRAQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHATFAL LFFFGHIWHG ARTLFRDIFA
     GIDPELDIQV EFGAFQKIGD PTTKRQVV