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PSBC_DAUCA
ID   PSBC_DAUCA              Reviewed;         473 AA.
AC   Q0G9W6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
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   Daucus carota (Wild carrot).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Danvers Half-long;
RX   PubMed=16945140; DOI=10.1186/1471-2164-7-222;
RA   Ruhlman T., Lee S.-B., Jansen R.K., Hostetler J.B., Tallon L.J., Town C.D.,
RA   Daniell H.;
RT   "Complete plastid genome sequence of Daucus carota: implications for
RT   biotechnology and phylogeny of angiosperms.";
RL   BMC Genomics 7:222-222(2006).
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; DQ898156; ABI32420.1; -; Genomic_DNA.
DR   RefSeq; YP_740113.1; NC_008325.1.
DR   AlphaFoldDB; Q0G9W6; -.
DR   SMR; Q0G9W6; -.
DR   EnsemblPlants; KZM81218; KZM81218; DCAR_032480.
DR   GeneID; 4266728; -.
DR   Gramene; KZM81218; KZM81218; DCAR_032480.
DR   OMA; WKDKNKM; -.
DR   OrthoDB; 620323at2759; -.
DR   GO; GO:0009533; C:chloroplast stromal thylakoid; IEA:EnsemblPlants.
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:0003729; F:mRNA binding; IEA:EnsemblPlants.
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_0000431139"
FT   CHAIN           15..473
FT                   /note="Photosystem II CP43 reaction center protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000361372"
FT   TRANSMEM        73..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        139..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        180..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        262..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        292..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        452..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   BINDING         367
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   473 AA;  51897 MW;  0A5D115650F5B1FF CRC64;
     MKTLYSLRRF YPVETLFNGT LALAGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI
     VFWAGGMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEVIDTFP YFVSGVLHLI
     SSAVLGFGGI YHALLGPETL EESFPFFGYV WKDRNKMTTI LGIHLILLGI GAFLLVFKAL
     YFGGVYDTWA PGGGDVRKIT NLTLNPSIIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL
     GSICIFGGIW HILTKPFAWA RRALVWSGEA YLSYSLAALS VFGFIACCFV WFNNTAYPSE
     FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD
     LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV
     SPRSWLATSH FVLGFFLFVG HLWHAGRARA AAAGFEKGID RDFEPVLSMT PLN
 
 
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