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PSBC_CYACA
ID   PSBC_CYACA              Reviewed;         460 AA.
AC   Q9TM46;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
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};
GN   Name=psbC {ECO:0000255|HAMAP-Rule:MF_01496};
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
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; AF022186; AAF13025.1; -; Genomic_DNA.
DR   RefSeq; NP_045020.2; NC_001840.1.
DR   PDB; 4YUU; X-ray; 2.77 A; C1/C2/c1/c2=1-460.
DR   PDBsum; 4YUU; -.
DR   AlphaFoldDB; Q9TM46; -.
DR   SMR; Q9TM46; -.
DR   GeneID; 800249; -.
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   1: Evidence at protein level;
KW   3D-structure; Chlorophyll; Chloroplast; Chromophore; Manganese; Membrane;
KW   Metal-binding; Photosynthesis; Photosystem II; Plastid; Thylakoid;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..460
FT                   /note="Photosystem II CP43 reaction center protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000077511"
FT   TRANSMEM        60..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        126..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        167..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        249..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        279..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   TRANSMEM        439..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT   BINDING         354
FT                   /ligand="[CaMn4O5] cluster"
FT                   /ligand_id="ChEBI:CHEBI:189552"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
SQ   SEQUENCE   460 AA;  50471 MW;  4CA62E2DEF43D78D CRC64;
     MLFNKDKNNI GGRSIESTGF AWWSGNARLI NLSGKLLGAH VAHAGLIVFW TGAMTLFETS
     HFIPEKPLYE QGMILLPHLA TLGWGVAPGG EIVNTYPYFA TGVIHLVSSA VLGFGGIYHS
     IVGPDVLEDS FSFFGYDWRD KNKMTTILGI HLILLGIGAF LLVIKALFIG GIYDTWAPGG
     GDIRFITNPT LNPAIIFSYL LKSPFGGEGW IVGVNNMEDV IGGHIWIGVT CVIGGIWHIL
     TRPFSWARRA FVWSGEAYLS YSLGALALMG QTAAEYAWYN NTVYPSEFYG PTAAEASQAQ
     AFTFLVRDQR LGANIASTQG PTGLGKYLMR SPTGEVILGG ETMRFWDLRA PWLEPLRSSN
     GLDLNKIKND IQPWQERRAA EYMTHAPLGS LNSVGGVATE INSVNYVSPR SWLTTSHFFL
     GFFIFIGHLW HAGRARAAAA GFEKGINREN EPVLSMRPLD
 
 
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