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PSBC_MARPO
ID   PSBC_MARPO              Reviewed;         473 AA.
AC   P06414; P09360;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 112.
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   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6393057; DOI=10.1093/nar/12.24.9551;
RA   Umesono K., Inokuchi H., Ohyama K., Ozeki H.;
RT   "Nucleotide sequence of Marchantia polymorpha chloroplast DNA: a region
RT   possibly encoding three tRNAs and three proteins including a homologue of
RT   E. coli ribosomal protein S14.";
RL   Nucleic Acids Res. 12:9551-9565(1984).
RN   [2]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
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 [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2974085; DOI=10.1016/0022-2836(88)90002-2;
RA   Umesono K., Inokuchi H., Shiki Y., Takeuchi M., Chang Z., Fukuzawa H.,
RA   Kohchi T., Shirai H., Ohyama K., Ozeki H.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   II. Gene organization of the large single copy region from rps'12 to
RT   atpB.";
RL   J. Mol. Biol. 203:299-331(1988).
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}.
CC   -!- PTM: Phosphorylated on threonine residue(s).
CC       {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=CAA25802.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X04465; CAA28081.1; -; Genomic_DNA.
DR   EMBL; X01647; CAA25802.1; ALT_INIT; Genomic_DNA.
DR   PIR; A03474; F2LV44.
DR   RefSeq; NP_039295.1; NC_001319.1.
DR   AlphaFoldDB; P06414; -.
DR   SMR; P06414; -.
DR   PRIDE; P06414; -.
DR   GeneID; 2702544; -.
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_0000431165"
FT   CHAIN           15..473
FT                   /note="Photosystem II CP43 reaction center protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01496"
FT                   /id="PRO_0000077519"
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;  51786 MW;  769CD734575DB3AB CRC64;
     MKILYSQRRF YPVETLFNGT LALGGRDQET TGFAWWAGNA RLINLSGKLL GAHVAHAGLI
     VFWAGAMNLF EVAHFVPEKP MYEQGLILLP HLATLGWGVG PGGEIVDTFP YFVSGVLHLI
     SSAVLGFGGI YHALIGPETL EESFPFFGYV WKDKNKMTTI LGIHLILLGA GAFLLVFKAL
     YFGGIYDTWA PGGGDVRKIT NLTLSPGVIF GYLLKSPFGG EGWIVSVDNL EDIIGGHVWL
     GSICIFGGIW HILTKPFAWA RRALVWSGEA YLSYSLGAIA VFGFIACCFV WFNNTAYPSE
     FYGPTGPEAS QAQAFTFLVR DQRLGANVGS AQGPTGLGKY IMRSPTGEII FGGETMRFWD
     LRAPWLEPLR GPNGLDLSKL KKDIQPWQER RSAEYMTHAP LGSLNSVGGV ATEINAVNYV
     SPRSWLATSH FVLGFFFFVG HLWHAGRARA AAAGFEKGID RDFEPVLSMT PLN
 
 
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