PSBC_CUSOB
ID PSBC_CUSOB Reviewed; 473 AA.
AC A8W3I3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
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 Cuscuta obtusiflora (Peruvian dodder).
OG Plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Grammica; Cuscuta sect. Cleistogrammica.
OX NCBI_TaxID=437280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT "Complete plastid genome sequences suggest strong selection for retention
RT of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL BMC Plant Biol. 7:57-57(2007).
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 membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- CAUTION: Only inflorescences, fruits, starved seedlings and stressed
CC stem tips are green in this organism. {ECO:0000305}.
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DR EMBL; EU189133; ABW20558.1; -; Genomic_DNA.
DR RefSeq; YP_001531213.1; NC_009949.1.
DR AlphaFoldDB; A8W3I3; -.
DR SMR; A8W3I3; -.
DR GeneID; 5714802; -.
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:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule.
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 Acetylation; Chlorophyll; Chromophore; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Photosynthesis; Photosystem II; Plastid; Transmembrane;
KW Transmembrane helix.
FT PROPEP 1..14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000431136"
FT CHAIN 15..473
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000361366"
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:0000255|HAMAP-Rule:MF_01496"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
SQ SEQUENCE 473 AA; 51872 MW; E2988D1A6FB3192C CRC64;
MKTLYSLRRF SHVETLFNTT LAVAGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI
VFWAGAMNLF EVAHFGPEKP MYEQGLILLP HLATLGWGVG PGGEIIDTFP YFVSGVLHLI
SSAVLGFGGI YHALLGPEII EESFPLFRYV WKDRNKMTTI LGIHLILLGL GAFLLVFKAL
YFGGVYDTWA PGGGDVRKIT NLTLSPSIIF GFLLKSPFGG DGWIVSVDDL EDIIGGHVWV
GSICIVGGIW HILTKPFAWA RRALVWSGEA YLSYSLGALS IFGFTACCFV WFNNTAYPSE
FYGPTGPEAS QAQAFTFLVR DQRLGANVGA AQGPTGLGKY LMRSPTGEVI FGGETMRFWD
LRAPWLEPLR GPNGLDLNRL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV
SPRSWLATSH FCLGFFFFVG HLWHAGRARA AAAGFEKGID RDFEPVLSMT PLN
