PSBB_EUCGG
ID PSBB_EUCGG Reviewed; 508 AA.
AC Q49KX2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 Eucalyptus globulus subsp. globulus (Tasmanian blue gum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16303753; DOI=10.1093/dnares/dsi006;
RA Steane D.A.;
RT "Complete nucleotide sequence of the chloroplast genome from the Tasmanian
RT blue gum, Eucalyptus globulus (Myrtaceae).";
RL DNA Res. 12:215-220(2005).
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; AY780259; AAX21053.1; -; Genomic_DNA.
DR RefSeq; YP_636325.1; NC_008115.1.
DR AlphaFoldDB; Q49KX2; -.
DR SMR; Q49KX2; -.
DR GeneID; 4108409; -.
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_0000359822"
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; 56082 MW; A63284DFAA2B2BF6 CRC64;
MGLPWYRVHT VVLNDPGRLL SVHIMHTALV AGWAGSMALY ELAVFDPSDP VLDPMWRQGM
FVIPFMTRLG ITNSWGGWSI TGGTITNPGI WSYEGVAGAH IVFSGLCFLA AIWHWVYWDL
EIFCDERTGK PSLDLPKIFG IHLFLSGVAC FGFGAFHVTG LYGPGIWVSD PYGLTGKVQP
VNPAWGVEGF DPFVPGGIAS HHIAAGTLGI LAGLFHLSVR PPQRLYKGLR MGNIETVLSS
SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDQGYF QQEIYRRVGA GLAKNQSLSE
AWSKIPEKLA FYDYIGNNPA KGGLFRAGSM DNGDGIAVGW LGHPIFRDKE GRELFVRRMP
TFFETFPVVL VDGDGIVRAD VPFRRAESKY SVEQVGVTVE FYGGELNGVS YSDPATVKKY
ARRAQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHASFAL LFFFGHIWHG ARTLFRDVFA
GIDPDLDAQV EFGAFQKLGD PTTRRQVV