PSBC_SPIOL
ID PSBC_SPIOL Reviewed; 473 AA.
AC P06003;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=Photosystem II 44 kDa chlorophyll apoprotein {ECO:0000303|PubMed:24177999, ECO:0000303|PubMed:6096808};
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6096808; DOI=10.1093/nar/12.23.8819;
RA Holschuh K., Bottomley W., Whitfeld P.R.;
RT "Structure of the spinach chloroplast genes for the D2 and 44 kd reaction-
RT centre proteins of photosystem II and for tRNASer (UGA).";
RL Nucleic Acids Res. 12:8819-8834(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=24177999; DOI=10.1007/bf00395705;
RA Alt J., Morris J., Westhoff P., Herrmann R.G.;
RT "Nucleotide sequence of the clustered genes for the 44kd chlorophyll a
RT apoprotein and the '32kd'-like protein of the photosystem II reaction
RT center in the spinach plastid chromosome.";
RL Curr. Genet. 8:597-606(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [4]
RP PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION, ACETYLATION AT
RP THR-15, AND PHOSPHORYLATION AT THR-15.
RX PubMed=3121625; DOI=10.1016/s0021-9258(19)57275-1;
RA Michel H., Hunt D.F., Shabanowitz J., Bennett J.;
RT "Tandem mass spectrometry reveals that three photosystem II proteins of
RT spinach chloroplasts contain N-acetyl-O-phosphothreonine at their NH2
RT termini.";
RL J. Biol. Chem. 263:1123-1130(1988).
RN [5]
RP SUSCEPTIBILITY TO OXIDATION, AND MUTAGENESIS OF TRP-365.
RX PubMed=12417747; DOI=10.1073/pnas.232591599;
RA Anderson L.B., Maderia M., Ouellette A.J., Putnam-Evans C., Higgins L.,
RA Krick T., MacCoss M.J., Lim H., Yates J.R. III, Barry B.A.;
RT "Posttranslational modifications in the CP43 subunit of photosystem II.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14676-14681(2002).
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:0000255|HAMAP-Rule:MF_01496, ECO:0000269|PubMed:3121625}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- PTM: Over time a tryptophan in the fifth lumenal loop is converted to
CC 2-hydroxy-2,3-dihydrotryptophan, 2-oxo-2,3-dihydrotryptophan, and
CC kynurenine by oxidizing species from the active site. This oxidation
CC targets the protein for turnover. {ECO:0000269|PubMed:12417747}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- CAUTION: The oxidation form of Trp-365 is subject of controversy and
CC could be the artifactual result of sample handling.
CC {ECO:0000305|PubMed:12417747}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M36833; AAA84631.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88722.1; -; Genomic_DNA.
DR PIR; B23038; F2SP44.
DR PIR; T08998; T08998.
DR RefSeq; NP_054929.1; NC_002202.1.
DR PDB; 3JCU; EM; 3.20 A; C/c=1-473.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; P06003; -.
DR SMR; P06003; -.
DR DIP; DIP-62009N; -.
DR IntAct; P06003; 1.
DR STRING; 3562.P06003; -.
DR CarbonylDB; P06003; -.
DR iPTMnet; P06003; -.
DR GeneID; 2715609; -.
DR KEGG; soe:2715609; -.
DR OrthoDB; 620323at2759; -.
DR Proteomes; UP000054095; 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 Direct protein sequencing; Manganese; Membrane; Metal-binding; Oxidation;
KW Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT PROPEP 1..14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:3121625"
FT /id="PRO_0000029430"
FT CHAIN 15..473
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000029431"
FT PROPEP 426..473
FT /evidence="ECO:0000269|PubMed:3121625"
FT /id="PRO_0000029432"
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 SITE 365
FT /note="Susceptible to oxidation"
FT /evidence="ECO:0000269|PubMed:12417747"
FT MOD_RES 15
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:3121625"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:3121625"
FT MUTAGEN 365
FT /note="W->A,C,L: Exhibits an increased rate of
FT photoinhibition relative to wild-type."
FT /evidence="ECO:0000269|PubMed:12417747"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 46..74
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 81..85
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 109..132
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 154..180
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3JCU"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 230..253
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 268..292
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 306..323
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 386..397
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 422..453
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 473 AA; 51834 MW; D5D9BD4E18752EBA CRC64;
MKTLYSLRRF YPVETLFNGT LTLAGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI
VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEVIDTFP YFVSGVLHLI
SSAVLGFGGI YHALLGPETL EESFPFFGYV WKDRNKMTTI LGIHLILLGI GAFLLVFKAL
YFGGVYDTWA PGGGDVRKIT NVTLSPSIIF GCLLKSPFGG EGWIVSVDDL EDIIGGHVWI
GVICILGGIW HILTKPFAWA RRALVWSGEA YLSYSLAALS VFGFIACCFV WFNNTAYPSE
FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD
LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV
SPRSWLSTSH FVLGFFLFVG HLWHAGRARA AAAGFEKGID RDFEPVLSMT PLN
