PSBC_GRATL
ID PSBC_GRATL Reviewed; 486 AA.
AC Q6B917;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
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}; OrderedLocusNames=Grc000036;
OS Gracilaria tenuistipitata var. liui (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX NCBI_TaxID=285951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT "Comparative analysis of the complete plastid genome sequence of the red
RT alga Gracilaria tenuistipitata var. liui provides insights into the
RT evolution of rhodoplasts and their relationship to other plastids.";
RL J. Mol. Evol. 59:464-477(2004).
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; AY673996; AAT79618.1; -; Genomic_DNA.
DR RefSeq; YP_063543.2; NC_006137.1.
DR AlphaFoldDB; Q6B917; -.
DR SMR; Q6B917; -.
DR GeneID; 2944079; -.
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 Chlorophyll; Chloroplast; Chromophore; Manganese; Membrane; Metal-binding;
KW Photosynthesis; Photosystem II; Plastid; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT PROPEP 1..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000431224"
FT CHAIN 29..486
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000361519"
FT TRANSMEM 86..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 152..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 193..209
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 275..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 305..320
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT TRANSMEM 465..481
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT BINDING 380
FT /ligand="[CaMn4O5] cluster"
FT /ligand_id="ChEBI:CHEBI:189552"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
SQ SEQUENCE 486 AA; 53671 MW; 40D5FC6A1520F3EB CRC64;
MKVFVHGWQH KISHTRILYS LRRFYHVETP FNQNIVSGRD LESTGFAWWS GNARLINVSG
KLLGAHVAHA GIMVFWTGAM TLFEVAHFIP EKPLYEQGFI LIPHLATLGW GVGPGGEIIN
IYPYFVVGIL HLISSAVLGF GGLYHALIGP DTLEESFPFF GYDWRDKNKM TTILGIHLVL
LGIGSFLLVI KALFFGGVYD TWAPGGGDVR LINNPTLNPA IIFGYVLKSP FGGDGWIVSV
NNMEDLIGGH VWIGVVCIAG GIWHILTKPF AWARRAFVWS GEAYLSYSLG ALSLMGLTAS
NYVWYNNTAY PSEFYGPTGP EASQAQAFTF LVRDQRLGAN VASAQGPTGL GKYLMRSPSG
EIIFGGETMR FWDLRAPWVE PLRGANGLDL NKIKNDIQPW QERRAAEYMT HAPLGSLNSV
GGVATEINSV NYVSPRSWLT TSHFFLGFFL FIGHLWHAGR ARAAAAGFEK GINRENEAVL
SMRPLD
