PSBC_MAIZE
ID PSBC_MAIZE Reviewed; 473 AA.
AC P48187;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [2]
RP PROTEIN SEQUENCE OF 15-26, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-15,
RP AND ACETYLATION AT THR-15.
RC STRAIN=cv. Olenka; TISSUE=Bundle sheath cell, and Mesophyll cell;
RX PubMed=22833285; DOI=10.1002/pmic.201200196;
RA Fristedt R., Wasilewska W., Romanowska E., Vener A.V.;
RT "Differential phosphorylation of thylakoid proteins in mesophyll and bundle
RT sheath chloroplasts from maize plants grown under low or high light.";
RL Proteomics 12:2852-2861(2012).
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}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
CC -!- PTM: Phosphorylated in both bundle sheath and mesophyll cells,
CC phosphorylation increases when cells are grown under high rather than
CC low light regimes (70 vs 900 umol photons/m-2/s).
CC {ECO:0000269|PubMed:22833285}.
CC -!- SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01496}.
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DR EMBL; X86563; CAA60271.1; -; Genomic_DNA.
DR PIR; S58537; S58537.
DR RefSeq; NP_043010.1; NC_001666.2.
DR AlphaFoldDB; P48187; -.
DR SMR; P48187; -.
DR STRING; 4577.GRMZM5G856777_P01; -.
DR iPTMnet; P48187; -.
DR PaxDb; P48187; -.
DR PRIDE; P48187; -.
DR GeneID; 845201; -.
DR KEGG; zma:845201; -.
DR MaizeGDB; 105980; -.
DR eggNOG; ENOG502QR3X; Eukaryota.
DR HOGENOM; CLU_028310_1_1_1; -.
DR OMA; WKDKNKM; -.
DR OrthoDB; 620323at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR ExpressionAtlas; P48187; baseline.
DR Genevisible; P48187; ZM.
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;
KW Direct protein sequencing; Membrane; Metal-binding; Phosphoprotein;
KW Photosynthesis; Photosystem II; Plastid; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:22833285"
FT /id="PRO_0000361510"
FT CHAIN 15..473
FT /note="Photosystem II CP43 reaction center protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT /id="PRO_0000077518"
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 ECO:0000269|PubMed:22833285"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01496,
FT ECO:0000269|PubMed:22833285"
SQ SEQUENCE 473 AA; 51900 MW; A53D37BA9FE8B86B CRC64;
MKILYSLRRF YHVETLFNGT FVLAGRDQET TGFPWWAGNA RLINLSGKLL GAHVAHAGLI
VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG SGGEVLDTFP YFVSGVLHLI
SSAVLGFGGI YHALLGPETL EESFPFFGYV WQDRNKMTTL LGIHLILLGL GAFLLVLKAL
YFGGVYDTWA PGGGDVRKIT NLTLSPGVIF GYLLKSPFGG EGWIVSVDDL EDIIGGHVWL
GSICVLGGIW HILTKPFAWA RRAFVWSGEA YLSYSLGALS VFGFIACCFV WFNNTAYPSE
FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY LMRSPTGEVI FGGETMRFWD
LRAPWLEPLR GPNGLDLSRL KKDGQPWQER RSGEYMTHAP LGSLNSVGGV ATEINAVNYV
SPRSWLATSH FVLGFFFFVG HLWHAGRARA AAAGFEKGID RDLEPVVYMT PLN
