PSBC_TETOB
ID PSBC_TETOB Reviewed; 461 AA.
AC Q1KVY2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
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 Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX NCBI_TaxID=3088;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 393;
RX PubMed=16638149; DOI=10.1186/1471-2148-6-37;
RA de Cambiaire J.-C., Otis C., Lemieux C., Turmel M.;
RT "The complete chloroplast genome sequence of the chlorophycean green alga
RT Scenedesmus obliquus reveals a compact gene organization and a biased
RT distribution of genes on the two DNA strands.";
RL BMC Evol. Biol. 6:37-37(2006).
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; DQ396875; ABD48224.1; -; Genomic_DNA.
DR RefSeq; YP_635942.1; NC_008101.1.
DR AlphaFoldDB; Q1KVY2; -.
DR SMR; Q1KVY2; -.
DR GeneID; 4099792; -.
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 3: Inferred from homology;
KW Acetylation; Chlorophyll; Chloroplast; Chromophore; 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_0000431206"
FT CHAIN 3..461
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000361491"
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; 50553 MW; 90A54A286B455BF8 CRC64;
METLFNGTLT VGGRDQESTG FAWWAGNARL INLSGKLLGA HVAHAGLIVY WAGAMNLFEV
AHFVPEKPMY EQGLILLPHL ATLGYGVGPG GEVIDTFPYF VSGVLHLISS AVLGFGGVYH
SLIGPETLEE SFPFFGYVWK DKNKMTNILG YHLIMLGIGA WLLVWKAMYF GGVYDTWAPG
GGDVRIITNP TTNAAVVFGY LLKSPFGGDG WIVSVDNMED IIGGHIWIGT LCILGGLWHI
YTTPWPWARR AFVWSGEAYL SYSLGAISLM GFIACCMSWF NNTAYPSEFY GPTGPEASQS
QAFTFLVRDQ RLGANVASAQ GPTGLGKYLM RSPTGEIIFG GETMRFWDFR GPWLEPLRGP
NGLDLNKLKN DIQPWQERRA AEYMTHAPLG SLNSVGGVAT EINAVNFVSP RSWLATSHFV
LGFFFFVGHL WHAGRARAAA AGFEKGIDRL DEPVLSMRPL D
