PSBC_CHLRE
ID PSBC_CHLRE Reviewed; 461 AA.
AC P10898; B7U1K6; Q9GGZ0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 AltName: Full=Protein P6 {ECO:0000303|PubMed:2663467};
DE Flags: Precursor;
GN Name=psbC {ECO:0000255|HAMAP-Rule:MF_01496};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-261.
RC STRAIN=137c / CC-125;
RX PubMed=2663467; DOI=10.1002/j.1460-2075.1989.tb03468.x;
RA Rochaix J.-D., Kuchka M., Mayfield S.P., Schirmer-Rahire M.,
RA Girard-Bascou J., Bennoun P.;
RT "Nuclear and chloroplast mutations affect the synthesis or stability of the
RT chloroplast psbC gene product in Chlamydomonas reinhardtii.";
RL EMBO J. 8:1013-1021(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-336.
RC STRAIN=137c / CC-125;
RX PubMed=11083939; DOI=10.1006/mpev.2000.0831;
RA Nozaki H., Misawa K., Kajita T., Kato M., Nohara S., Watanabe M.M.;
RT "Origin and evolution of the colonial Volvocales (Chlorophyceae) as
RT inferred from multiple, chloroplast gene sequences.";
RL Mol. Phylogenet. Evol. 17:256-268(2000).
RN [4]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
RN [5]
RP SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=1885590; DOI=10.1016/s0021-9258(18)55345-x;
RA de Vitry C., Diner B.A., Popo J.-L.;
RT "Photosystem II particles from Chlamydomonas reinhardtii. Purification,
RT molecular weight, small subunit composition, and protein phosphorylation.";
RL J. Biol. Chem. 266:16614-16621(1991).
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 ECO:0000269|PubMed:1885590}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:1885590}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- PTM: Phosphorylated in vitro (PubMed:1885590).
CC {ECO:0000269|PubMed:1885590}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
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DR EMBL; X13879; CAA32084.2; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50153.1; -; Genomic_DNA.
DR EMBL; AB044528; BAB18454.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00966.1; -; Genomic_DNA.
DR PIR; S04025; S04025.
DR RefSeq; NP_958422.1; NC_005353.1.
DR PDB; 6KAC; EM; 2.70 A; C/c=1-461.
DR PDB; 6KAD; EM; 3.40 A; C/c=1-461.
DR PDB; 6KAF; EM; 3.73 A; C/c=1-461.
DR PDBsum; 6KAC; -.
DR PDBsum; 6KAD; -.
DR PDBsum; 6KAF; -.
DR AlphaFoldDB; P10898; -.
DR SMR; P10898; -.
DR STRING; 3055.DAA00966; -.
DR PaxDb; P10898; -.
DR PRIDE; P10898; -.
DR GeneID; 2716963; -.
DR KEGG; cre:ChreCp066; -.
DR eggNOG; ENOG502QR3X; Eukaryota.
DR HOGENOM; CLU_028310_1_1_1; -.
DR InParanoid; P10898; -.
DR OrthoDB; 620323at2759; -.
DR BioCyc; MetaCyc:CHRECP066-MON; -.
DR Proteomes; UP000006906; Chloroplast.
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; Acetylation; Chlorophyll; Chloroplast; Chromophore;
KW Manganese; Membrane; Metal-binding; Phosphoprotein; Photosynthesis;
KW Photosystem II; Plastid; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT PROPEP 1..2
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000431124"
FT CHAIN 3..461
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000077509"
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:0000255|HAMAP-Rule:MF_01496"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT MUTAGEN 261
FT /note="S->SLS: In MA16; destabilizes protein leading to
FT loss of PSII."
FT /evidence="ECO:0000269|PubMed:2663467"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 34..61
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 69..73
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 97..122
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 142..168
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 218..240
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 256..280
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 294..311
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 410..441
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:6KAC"
SQ SEQUENCE 461 AA; 50639 MW; EAED8FA470B6E10F CRC64;
METLFNGTLT VGGRDQETTG FAWWSGNARL INLSGKLLGA HVAHAGLIVF WAGAMNLFEV
SHFVPEKPMY EQGLILLPHI ATLGYGVGPG GEIIDTFPYF VSGVLHLISS AVLGFGGVYH
SLIGPETLEE SYPFFGYVWK DKNKMTNILG YHLIMLGLGA WLLVWKAMYF GGVYDTWAPG
GGDVRVITNP TTNAAVIFGY LVKSPFGGDG WICSVDNMED IIGGHIWIGT LEILGGIWHI
YTTPWPWARR AFVWSGEAYL SYSLGAIGVM GFIACCMSWF NNTAYPSEFY GPTGPEASQS
QAFTFLVRDQ RLGANVASAQ GPTGLGKYLM RSPTGEIIFG GETMRFWDFR GPWLEPLRGP
NGLDLNKLKN DIQPWQERRA AEYMTHAPLG SLNSVGGVAT EINAVNFVSP RSWLACSHFC
LGFFFFIGHL WHAGRARAAA AGFEKGIDRF DEPVLSMRPL D
