PSBB_SPIOL
ID PSBB_SPIOL Reviewed; 508 AA.
AC P04160; Q36791; Q6EYE1; Q9M3K4;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 110.
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6324128; DOI=10.1093/nar/12.6.2837;
RA Morris J., Herrmann R.G.;
RT "Nucleotide sequence of the gene for the P680 chlorophyll alpha apoprotein
RT of the photosystem II reaction center from spinach.";
RL Nucleic Acids Res. 12:2837-2850(1984).
RN [2]
RP SEQUENCE REVISION.
RA Morris J., Herrmann R.G.;
RL Submitted (JUN-1984) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RA Witty M., Barber J., Hiller R.G.;
RT "Spinach CP47 is not anomalous among higher plants.";
RL (er) Plant Gene Register PGR96-071(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-508.
RA Graham S.W., Rai H.S., Ikegami K., Reeves P.A., Olmstead R.G.;
RT "Parsing out signal and noise for seed-plant phylogenetic inference.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ASPARTYL ALDEHYDE AT ASP-348, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=15237995; DOI=10.1021/ja0478781;
RA Anderson L.B., Ouellette A.J., Eaton-Rye J., Maderia M., MacCoss M.J.,
RA Yates J.R. III, Barry B.A.;
RT "Evidence for a post-translational modification, aspartyl aldehyde, in a
RT photosynthetic membrane protein.";
RL J. Am. Chem. Soc. 126:8399-8405(2004).
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, ECO:0000269|PubMed:15237995}; Multi-
CC pass membrane protein {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; X02945; CAA26691.1; -; Genomic_DNA.
DR EMBL; X98877; CAA67379.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88753.1; -; Genomic_DNA.
DR EMBL; AF528912; AAQ09432.1; -; Genomic_DNA.
DR PIR; A03470; QJSP6A.
DR RefSeq; NP_054960.1; NC_002202.1.
DR PDB; 3JCU; EM; 3.20 A; B/b=1-508.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; P04160; -.
DR SMR; P04160; -.
DR DIP; DIP-62008N; -.
DR IntAct; P04160; 1.
DR STRING; 3562.P04160; -.
DR PRIDE; P04160; -.
DR GeneID; 2715608; -.
DR KEGG; soe:2715608; -.
DR OrthoDB; 528752at2759; -.
DR Proteomes; UP000054095; Chloroplast.
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 1: Evidence at protein level;
KW 3D-structure; Chlorophyll; Chloroplast; Chromophore; Membrane;
KW Photosynthesis; Photosystem II; Plastid; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..508
FT /note="Photosystem II CP47 reaction center protein"
FT /id="PRO_0000077498"
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"
FT MOD_RES 348
FT /note="Aspartyl aldehyde"
FT /evidence="ECO:0000269|PubMed:15237995"
FT CONFLICT 1
FT /note="M -> MKIS (in Ref. 3; CAA67379)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="G -> S (in Ref. 1; CAA26691)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..183
FT /note="SP -> CS (in Ref. 1; CAA26691)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="G -> R (in Ref. 1; CAA26691)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="P -> S (in Ref. 1; CAA26691)"
FT /evidence="ECO:0000305"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 16..44
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 93..116
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 135..155
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 196..218
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 234..258
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 447..474
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 476..480
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 508 AA; 56153 MW; B3B58F11C5582CF5 CRC64;
MGLPWYRVHT VVLNDPGRLI SVHIMHTALV AGWAGSMALY ELAVFDPSDP VLDPMWRQGM
FVIPFMTRLG ITNSWGGWSI TGGTITDPGI WSYEGVAGAH IMFSGLCFLA AIWHWVYWDL
EIFSDERTGK PSLDLPKIFG IHLFLSGVAC FGFGAFHVTG LYGPGIWVSD PYGLTGKVQP
VSPAWGVEGF DPFVPGGIAS HHIAAGTLGI LAGLFHLSVR PPQRLYKGLR MGNIETVLSS
SIAAVFFAAF VVAGTMWYGS ATTPIELFGP TRYQWDQGYF QQEIYRRVSA GLAENQSFSE
AWSKIPEKLA FYDYIGNNPA KGGLFRAGSM DNGDGIAVGW LGHPIFRDKE GRELFVRRMP
TFFETFPVVL IDGDGIVRAD VPFRRAESKY SVEQVGVTVE FYGGELNGVS YSDPATVKKY
ARRAQLGEIF ELDRATLKSD GVFRSSPRGW FTFGHASFAL LFFFGHIWHG SRTLFRDVFA
GIDPDLDVQV EFGAFQKIGD PTTRRQGV
