PSBC_CYAPA
ID PSBC_CYAPA Reviewed; 461 AA.
AC P48104;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Cyanophora paradoxa.
OG Plastid; Cyanelle.
OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX NCBI_TaxID=2762;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA Bryant D.A.;
RT "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL Plant Mol. Biol. Rep. 13:327-332(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT genetic complexity of a primitive plastid.";
RL (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL (eds.);
RL Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
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, cyanelle thylakoid membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC 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; U30821; AAA81279.1; -; Genomic_DNA.
DR PIR; T06936; T06936.
DR RefSeq; NP_043248.3; NC_001675.1.
DR AlphaFoldDB; P48104; -.
DR SMR; P48104; -.
DR GeneID; 801626; -.
DR GO; GO:0033115; C:cyanelle 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 3: Inferred from homology;
KW Acetylation; Chlorophyll; Chromophore; Cyanelle; Manganese; Membrane;
KW Metal-binding; Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Thylakoid; Transmembrane; Transmembrane helix.
FT PROPEP 1..2
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000431222"
FT CHAIN 3..461
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000077512"
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:0000250, ECO:0000255|HAMAP-Rule:MF_01496"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01496"
SQ SEQUENCE 461 AA; 50402 MW; 62664E239E13B9C1 CRC64;
METLFNSSVA VSGRDQQSTG FAWWSGNARL INLSGKLLGA HVAHAGLIVF WTGAMTLFEV
AHFIPEKPMY EQGLILLPHL ATLGWGVGPG GEVIDVYPYF VVGVLHLVSS AVLGFGGLYH
AIIGPEVLEE SFPFFGYDWK DKNKMTTIIG IHLILLGSGA LLLVLKAMFF GGVYDTWAPG
GGDVRVISNP TLNPTVIFSY ITKSPWGGDG WIVSVDNMED IIGGHIWLAF ICIIGGVWHI
LTKPFSWARR ALVWSGEAYL SYSLAALALM GFIANCFVWF NNTAYPSEFF GPTGPEASQA
QAFTFLVRDQ RLGANVGSAQ GPTGLGKYLM RSPSGEIIFG GETMRFWDTR APWLEPLRGA
NGLDLTKIKY DIQPWQERRA AEYMTHAPLG SLNSVGGVAT EINSVNYVSP RSWLSTSHFV
LGFFLFIGHL WHAGRARAAS GGFEKGLDRE NEPVLSMKLL D
