PSBB_CHLRE
ID PSBB_CHLRE Reviewed; 508 AA.
AC P37255; B7U1H4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX PubMed=16668833; DOI=10.1104/pp.98.4.1541;
RA Berry-Lowe S.L., Johnson C.H., Schmidt G.W.;
RT "Nucleotide sequence of the psbB gene of Chlamydomonas reinhardtii
RT chloroplasts.";
RL Plant Physiol. 98:1541-1543(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 492-508.
RX PubMed=1371579; DOI=10.1007/bf00292715;
RA Monod C., Goldschmidt-Clermont M., Rochaix J.-D.;
RT "Accumulation of chloroplast psbB RNA requires a nuclear factor in
RT Chlamydomonas reinhardtii.";
RL Mol. Gen. Genet. 231:449-459(1992).
RN [4]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
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; M84022; AAA84154.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50121.1; -; Genomic_DNA.
DR EMBL; X64066; CAA45421.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00933.1; -; Genomic_DNA.
DR PIR; S20490; S20490.
DR PIR; T07985; T07985.
DR RefSeq; NP_958388.1; NC_005353.1.
DR PDB; 6KAC; EM; 2.70 A; B/b=1-508.
DR PDB; 6KAD; EM; 3.40 A; B/b=1-508.
DR PDB; 6KAF; EM; 3.73 A; B/b=1-508.
DR PDBsum; 6KAC; -.
DR PDBsum; 6KAD; -.
DR PDBsum; 6KAF; -.
DR AlphaFoldDB; P37255; -.
DR SMR; P37255; -.
DR STRING; 3055.DAA00933; -.
DR PaxDb; P37255; -.
DR PRIDE; P37255; -.
DR GeneID; 2717002; -.
DR KEGG; cre:ChreCp032; -.
DR eggNOG; ENOG502QRV6; Eukaryota.
DR HOGENOM; CLU_028227_2_0_1; -.
DR InParanoid; P37255; -.
DR OrthoDB; 528752at2759; -.
DR BioCyc; MetaCyc:CHRECP032-MON; -.
DR Proteomes; UP000006906; 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_0000077478"
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 HELIX 5..11
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 16..44
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 93..116
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 135..155
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 196..218
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 235..258
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 427..437
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 447..474
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 477..480
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:6KAC"
SQ SEQUENCE 508 AA; 56106 MW; 17F4959510C59639 CRC64;
MGLPWYRVHT VVINDPGRLI SVHLMHTALV SGWAGSMALF EISVFDPSDP VLNPMWRQGM
FVLPFMTRLG ITQSWGGWTI SGETATNPGI WSYEGVAAAH IILSGALFLA SVWHWTYWDL
ELFRDPRTGK TALDLPKIFG IHLFLSGLLC FGFGAFHVTG VFGPGIWVSD PYGLTGRVQP
VAPSWGADGF DPYNPGGIAS HHIAAGILGV LAGLFHLCVR PSIRLYFGLS MGSIETVLSS
SIAAVFWAAF VVAGTMWYGS AATPIELFGP TRYQWDQGFF QQEIQKRVQA SLAEGASLSD
AWSRIPEKLA FYDYIGNNPA KGGLFRTGAM NSGDGIAVGW LGHASFKDQE GRELFVRRMP
TFFETFPVLL LDKDGIVRAD VPFRKAESKY SIEQVGVSVT FYGGELDGLT FTDPATVKKY
ARKAQLGEIF EFDRSTLQSD GVFRSSPRGW FTFGHVCFAL LFFFGHIWHG ARTIFRDVFA
GIDDDINDQV EFGKYKKLGD TSSLREAF
