PSBB_CYCTA
ID PSBB_CYCTA Reviewed; 508 AA.
AC A6H5K7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
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 Cycas taitungensis (Prince sago) (Cycas taiwaniana).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Cycadidae; Cycadales; Cycadaceae; Cycas.
OX NCBI_TaxID=54799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17383970; DOI=10.1093/molbev/msm059;
RA Wu C.-S., Wang Y.-N., Liu S.-M., Chaw S.-M.;
RT "Chloroplast genome (cpDNA) of Cycas taitungensis and 56 cp protein-coding
RT genes of Gnetum parvifolium: insights into cpDNA evolution and phylogeny of
RT extant seed plants.";
RL Mol. Biol. Evol. 24:1366-1379(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}.
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DR EMBL; AP009339; BAF64973.1; -; Genomic_DNA.
DR RefSeq; YP_001312232.1; NC_009618.1.
DR GeneID; 5309472; -.
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_0000359817"
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; 56077 MW; C31CE0DCF747E988 CRC64;
MGLPWYRVHT VVLNDPGRLL SVHIMHTALV SGWAGSMALY ELAVFDPSDP VLDPMWRQGM
FVIPFMTRLG INNSWGGWSI TGETVTNPGL WSYEGVAGAH IVFSGLCFLA AIWHWVYWDL
DIFCDERTGK PSLDLPKIFG IHLFLSGVAC FGSGAFHVTG LYGPGIWVSD PYGLTGKIQP
VNPAWGAEGF DPFVPGGIAS HHIAAGILGI LAGLFHLSVR PPQRLYKGLR MGNIETVLSS
SIAAVFFAAF IVAGTMWYGS ATAPVELFGP TRYQWDQGYF QQEIDRRVRA GLSENLSLSE
AWSKIPEKLA FYDYIGNNPA KGGLFRAGAM DNGDGIAVGW LGHPIFRDKE GHELFVRRMP
TFFETFPVVL VDEEGIVKAD VPFRRAESKY SVEQVGVTVE FYGGELDGVS FGDPATVKKY
ARRAQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHATFAL LFFFGHIWHG ARTLFRDVFA
GIDPDLDAQV EFGAFQXLGD PTTKRQIV