PSBC_SECCE
ID PSBC_SECCE Reviewed; 473 AA.
AC P10804;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 102.
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};
OS Secale cereale (Rye).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Secale.
OX NCBI_TaxID=4550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2644624; DOI=10.1093/nar/17.2.798;
RA Bukharov A.A., Kolosov V.L., Klezovich O.N., Zolotarev A.S.;
RT "Nucleotide sequence of rye chloroplast DNA fragment, comprising psbD, psbC
RT and trnS genes.";
RL Nucleic Acids Res. 17:798-798(1989).
RN [2]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=9512353; DOI=10.1016/s0014-5793(98)00088-x;
RA Pursiheimo S., Rintamaeki E., Baena-Gonzalez E., Aro E.-M.;
RT "Thylakoid protein phosphorylation in evolutionally divergent species with
RT oxygenic photosynthesis.";
RL FEBS Lett. 423:178-182(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2080928;
RA Bukharov A.A., Kolosov V.L., Zolotarev A.S.;
RT "Rye photosystem II. Nucleotide sequence of the psbC gene coding 43-kDa
RT chlorophyll(a)-binding proteins.";
RL Bioorg. Khim. 16:1210-1217(1990).
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:9512353}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01496, ECO:0000305}.
CC -!- PTM: Phosphorylated on threonine residue(s); phosphorylation increases
CC with increasing light levels. {ECO:0000269|PubMed:9512353}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC35458.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X13366; CAA31744.1; -; Genomic_DNA.
DR EMBL; X13366; CAC35458.1; ALT_INIT; Genomic_DNA.
DR PIR; S03436; S03436.
DR AlphaFoldDB; P10804; -.
DR SMR; P10804; -.
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 Acetylation; Chlorophyll; Chloroplast; Chromophore; Manganese; Membrane;
KW Metal-binding; Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Thylakoid; Transmembrane; Transmembrane helix.
FT PROPEP 1..14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000431207"
FT CHAIN 15..473
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000077527"
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:0000255|HAMAP-Rule:MF_01496"
SQ SEQUENCE 473 AA; 52075 MW; 49AFA1D4C49EDDF7 CRC64;
MKILYSLRRF YHVETLFNGT FVLAGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI
VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEVLDTFP YFVSGVLHLI
SSAVLGFGGI YHALLGPETL EESFPFFGYV WKDRNKMTTI LGIHLILLGL GAFLLVLKAL
YFGGVYDTWA PGGGDVRKIT NLTLSPSVIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL
GFICVFGGIW HILTKPFAWA RRAFVWSGEA YLSYSLAALS VFGFIACCFV WFNNTAYSSE
FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD
LRAPWLEPLR GPNGLDLSRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV
SPRSWLSTSH FVLGFFPFVG HLWHAGRARA AAAGFEKGID RDLEPVLYMN PLN
