PSBB_BARVE
ID PSBB_BARVE Reviewed; 508 AA.
AC A4QKD1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 49.
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 Barbarea verna (Early yellowrocket) (Erysimum vernum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Barbarea.
OX NCBI_TaxID=50458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hosouchi T., Tsuruoka H., Kotani H.;
RT "Sequencing analysis of Barbarea verna chloroplast DNA.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; AP009370; BAF50136.1; -; Genomic_DNA.
DR RefSeq; YP_001123312.1; NC_009269.1.
DR AlphaFoldDB; A4QKD1; -.
DR SMR; A4QKD1; -.
DR PRIDE; A4QKD1; -.
DR GeneID; 4961913; -.
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_0000359798"
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; 56069 MW; 7D344030C774375D CRC64;
MGLPWYRVHT VVLNDPGRLL SVHIMHTALV AGWAGSMALY ELAVFDPSDP VLDPMWRQGM
FVIPFMTRLG ITNSWGGWNI TGGTITNPGL WSYEGVAGAH IVFSGLCFLA AIWHWVYWDL
EIFCDERTGK PSLDLPKIFG IHLFLSGVAC FGFGAFHVTG LYGPGIWVSD PYGLTGKVQP
VNPAWGVEGF DPFVPGGIAS HHIAAGTLGI LAGLFHLSVR PPQRLYKGLR MGNIETVLSS
SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDQGYF QQEIYRRVSA GLAENQSLSE
AWSKIPEKLA FYDYIGNNPA KGGLFRAGSM DNGDGIAVGW LGHPVFRNKE GRELFVRRMP
TFFETFPVVL VDGDGIVRAD VPFRRAESKY SVEQVGVTVE FYGGELNGVS YSDPATVKKY
ARRAQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHASFAL LFFFGHIWHG ARTLFRDVFA
GIDPDLDAQV EFGAFQKLGD PTTKRQAV