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PSBC_EUGGR
ID   PSBC_EUGGR              Reviewed;         461 AA.
AC   P05700;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Photosystem II CP43 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE   AltName: Full=PSII 43 kDa protein {ECO:0000255|HAMAP-Rule:MF_01496};
DE   AltName: Full=Protein CP-43 {ECO:0000255|HAMAP-Rule:MF_01496};
DE   Flags: Precursor;
GN   Name=psbC {ECO:0000255|HAMAP-Rule:MF_01496};
OS   Euglena gracilis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z / UTEX 753;
RX   PubMed=8346031; DOI=10.1093/nar/21.15.3537;
RA   Hallick R.B., Hong L., Drager R.G., Favreau M.R., Monfort A., Orsat B.,
RA   Spielmann A., Stutz E.;
RT   "Complete sequence of Euglena gracilis chloroplast DNA.";
RL   Nucleic Acids Res. 21:3537-3544(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RX   PubMed=8193167; DOI=10.1016/0167-4781(94)90102-3;
RA   Orsat B., Spielmann A., Marc-Martin S., Lemberger T., Stutz E.;
RT   "Analysis of the 22 kbp long psbD-psbC gene cluster of Euglena gracilis
RT   chloroplast DNA: evidence for overlapping transcription units undergoing
RT   differential processing.";
RL   Biochim. Biophys. Acta 1218:75-81(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-119.
RX   PubMed=3129199; DOI=10.1007/bf00389423;
RA   Montandon P.-E., Vasserot A., Stutz E.;
RT   "Euglena gracilis chloroplast DNA: analysis of a 1.6 kb intron of the psb C
RT   gene containing an open reading frame of 458 codons.";
RL   Curr. Genet. 11:35-39(1986).
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_01496}.
CC   -!- COFACTOR:
CC       Note=Binds multiple chlorophylls and provides some of the ligands for
CC       the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also
CC       provide a ligand for a Cl- that is required for oxygen evolution. PSII
CC       binds additional chlorophylls, carotenoids and specific lipids.
CC       {ECO:0000255|HAMAP-Rule:MF_01496};
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_01496}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496}; Multi-pass membrane
CC       protein {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496}.
CC   -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01496}.
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DR   EMBL; Z11874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X04509; CAA28193.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X70810; CAA50079.1; -; Genomic_DNA.
DR   PIR; S34498; S34498.
DR   RefSeq; NP_041892.1; NC_001603.2.
DR   AlphaFoldDB; P05700; -.
DR   SMR; P05700; -.
DR   GeneID; 807496; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR   Gene3D; 1.10.10.670; -; 1.
DR   HAMAP; MF_01496; PSII_PsbC_CP43; 1.
DR   InterPro; IPR000932; PS_antenna-like.
DR   InterPro; IPR036001; PS_II_antenna-like_sf.
DR   InterPro; IPR005869; PSII_PsbC.
DR   InterPro; IPR044900; PSII_PsbC_sf.
DR   PANTHER; PTHR33180; PTHR33180; 1.
DR   Pfam; PF00421; PSII; 1.
DR   SUPFAM; SSF161077; SSF161077; 1.
DR   TIGRFAMs; TIGR01153; psbC; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chlorophyll; Chloroplast; Chromophore; Manganese; Membrane;
KW   Metal-binding; Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW   Thylakoid; Transmembrane; Transmembrane helix.
FT   PROPEP          1..2
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000431221"
FT   CHAIN           3..461
FT                   /note="Photosystem II CP43 reaction center protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000077513"
FT   TRANSMEM        61..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        127..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        168..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        250..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        280..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        440..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   BINDING         355
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   MOD_RES         3
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496"
FT   MOD_RES         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496"
SQ   SEQUENCE   461 AA;  50710 MW;  6136358EFC4C0A4E CRC64;
     METLFNKKLT VGGRDQESTG FAWWAGNARL INVSGKLLGA HVAHAGLIVF WTGAMNLFEV
     AHFVPQKPMY EQGLILLPHL ATLGFGVGFD GIVLDTYPFF VCGVLHLISS AVLGFGGVFH
     SLAGPDTLEE SFRFFGYTWK RKKKLAAILG IHLCFLGLGA LLLAWKAMYG GGVYDTWWPG
     GGDVRSITNP TLNPFIIFGY LVKSPFGGEG WIVSVDSMEY VIGGHIWIGI LLVSGGFWHI
     CSRPSPWVVR TFVWSGEAYL SYSLGAVATM GFIAVPMVWF NNTVYPSEFY GPTGPEASQA
     QAFTFLIRDQ RLGTNIASAQ GPTGLGKYLM KSPTGEIIFG GETMRFWDFR GPWLEPLRGP
     NGLDLNKLKN DVQPWQERRA AEYMTHAPLG SLNSVGGVAT EINAVNFVNP RSWLATSHFV
     LAFFFFVGHL WHAGRARAAA IGFEKGIDRS REIARKLKPL D
 
 
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