PSBC_PEA
ID PSBC_PEA Reviewed; 473 AA.
AC P06004;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 98.
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|Ref.2};
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 Pisum sativum (Garden pea).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Rosakrone;
RX AGRICOLA=IND84114033; DOI=10.1007/BF00029654;
RA Rasmussen O.F., Bookjans G., Stutmann B.M., Henningsen K.W.;
RT "Localization and nucleotide sequence of the gene for the membrane
RT polypeptide D2 from pea chloroplast DNA.";
RL Plant Mol. Biol. 3:191-199(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Rosakrone;
RX AGRICOLA=IND87019930; DOI=10.1007/BF00034943;
RA Bookjans G.B., Stummann B.M., Rasmussen O.F., Henningsen K.W.;
RT "Structure of a 3.2 kb region of pea chloroplast DNA containing the gene
RT for the 44 kD photosystem II polypeptide.";
RL Plant Mol. Biol. 6:359-366(1986).
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; M27309; AAB59336.1; -; Genomic_DNA.
DR RefSeq; YP_003587541.1; NC_014057.1.
DR PDB; 5XNL; EM; 2.70 A; C/c=1-473.
DR PDB; 5XNM; EM; 3.20 A; C/c=1-473.
DR PDB; 6YP7; EM; 3.80 A; C/c=24-473.
DR PDBsum; 5XNL; -.
DR PDBsum; 5XNM; -.
DR PDBsum; 6YP7; -.
DR AlphaFoldDB; P06004; -.
DR SMR; P06004; -.
DR GeneID; 9073078; -.
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; Thylakoid; Transmembrane; Transmembrane helix.
FT PROPEP 1..14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000431197"
FT CHAIN 15..473
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000077524"
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"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 46..73
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:5XNL"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 109..134
FT /evidence="ECO:0007829|PDB:5XNL"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5XNL"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 154..180
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 230..253
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 268..292
FT /evidence="ECO:0007829|PDB:5XNL"
FT TURN 295..301
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 306..323
FT /evidence="ECO:0007829|PDB:5XNL"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5XNM"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:5XNL"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 386..397
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 422..453
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:5XNL"
SQ SEQUENCE 473 AA; 51988 MW; 13076F2555CC4971 CRC64;
MKTLYSLRRF YHVETLFNGT LALTGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI
VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEVIDTFP YFVSGVLHLI
SSAVLGFGGI YHALLGPETL EESFPFFGYV WKDRNKMTTI LGIHLILLGI GSFLLVFKAF
YFGGIYDTWA PGGGDVRKIT NFTLSPSILF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL
GSICILGGIW HILTKPFAWA RRALVWSGEA YLSYSLGALA VFGFIACCFV WFNNTAYPSE
FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD
LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV
SPRSWLATSH FVLGFFLFVG HLWHAGRARA AAAGFEKGID RDFEPVLSMT PLN
