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PSBC_TRICV
ID   PSBC_TRICV              Reviewed;         471 AA.
AC   P49472;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
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   Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC   Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX   NCBI_TaxID=1514140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT   "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT   sinensis.";
RL   Plant Mol. Biol. Rep. 13:336-342(1995).
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; Z67753; CAA91720.1; -; Genomic_DNA.
DR   PIR; S78347; S78347.
DR   AlphaFoldDB; P49472; -.
DR   SMR; P49472; -.
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..14
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000431227"
FT   CHAIN           15..471
FT                   /note="Photosystem II CP43 reaction center protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000077521"
FT   TRANSMEM        71..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        137..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        178..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        260..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        290..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        450..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   BINDING         365
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   MOD_RES         15
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496"
FT   MOD_RES         15
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496"
SQ   SEQUENCE   471 AA;  51879 MW;  340A424CE2AD2CFC CRC64;
     MKTLYSLRRY YHVETPFNSS IAGRDIESTG FAWWSGNARL INVSGKLLGA HVAHAGLMVF
     WAGAMVLFEV SHFVPEKPTY EQGFILIQHL ATLGYGIGPG GEITSTVPYF AVGVIHLISS
     AVLGFGGIYH SLLGPDTLEE SFPFFGYDWR DKNKMTTILG IHLCLLGVGS FLLVIKAMYL
     GGVYDTWAPG GGDVRLITTP TLNPIVIFGY VFRSPFGGDG WVVSVNNMED IIGGHIWVGL
     LCIIGGIWHI FTKPFAWARR AFVWSGEAYL SYSLAAISLM GFTAALYSWY NNTAYPSELY
     GPTGPEASQS QAFTFLVRDQ RLGANVSSAQ GPTGLGKYLM RSPSGEIIFG GETMRFWDLR
     APWVEPLRGP NGLDINKIKN DIQPWQERRA AEYMTHAPLG SLNSVGGVAT EINSVNYVSP
     RSWLCCSHFF LAFFFLIGHW WHSGRARAAA AGFEKGINRA NEPVLSMRPI D
 
 
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