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PSBI_SPIOL
ID   PSBI_SPIOL              Reviewed;          36 AA.
AC   P62103; P09970;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Photosystem II reaction center protein I {ECO:0000255|HAMAP-Rule:MF_01316};
DE            Short=PSII-I {ECO:0000255|HAMAP-Rule:MF_01316};
DE   AltName: Full=PSII 4.8 kDa protein {ECO:0000255|HAMAP-Rule:MF_01316, ECO:0000303|PubMed:3058517};
GN   Name=psbI {ECO:0000255|HAMAP-Rule:MF_01316};
OS   Spinacia oleracea (Spinach).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX   PubMed=11292076; DOI=10.1023/a:1006478403810;
RA   Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA   Mache R.;
RT   "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT   sequence and gene organization.";
RL   Plant Mol. Biol. 45:307-315(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-20, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=3058517; DOI=10.1016/0014-5793(88)81039-1;
RA   Ikeuchi M., Inoue Y.;
RT   "A new photosystem II reaction center component (4.8 kDa protein) encoded
RT   by chloroplast genome.";
RL   FEBS Lett. 241:99-104(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-20, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=2644131; DOI=10.1016/0014-5793(89)80482-x;
RA   Ikeuchi M., Takio K., Inoue Y.;
RT   "N-terminal sequencing of photosystem II low-molecular-mass proteins. 5 and
RT   4.1 kDa components of the O2-evolving core complex from higher plants.";
RL   FEBS Lett. 242:263-269(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-5, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT
RP   MET-1, AND MASS SPECTROMETRY.
RX   PubMed=9632665; DOI=10.1074/jbc.273.26.16122;
RA   Zheleva D., Sharma J., Panico M., Morris H.R., Barber J.;
RT   "Isolation and characterization of monomeric and dimeric CP47-reaction
RT   center photosystem II complexes.";
RL   J. Biol. Chem. 273:16122-16127(1998).
CC   -!- FUNCTION: One of the components of the core complex of photosystem II
CC       (PSII), required for its stability and/or assembly. PSII is a light-
CC       driven water:plastoquinone oxidoreductase that uses light energy to
CC       abstract electrons from H(2)O, generating O(2) and a proton gradient
CC       subsequently used for ATP formation. It consists of a core antenna
CC       complex that captures photons, and an electron transfer chain that
CC       converts photonic excitation into a charge separation.
CC       {ECO:0000255|HAMAP-Rule:MF_01316}.
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_01316,
CC       ECO:0000269|PubMed:2644131, ECO:0000269|PubMed:3058517,
CC       ECO:0000269|PubMed:9632665}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01316, ECO:0000269|PubMed:2644131,
CC       ECO:0000269|PubMed:3058517, ECO:0000269|PubMed:9632665}; Single-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01316,
CC       ECO:0000305|PubMed:2644131, ECO:0000305|PubMed:3058517,
CC       ECO:0000305|PubMed:9632665}.
CC   -!- MASS SPECTROMETRY: Mass=4195.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9632665};
CC   -!- SIMILARITY: Belongs to the PsbI family. {ECO:0000255|HAMAP-
CC       Rule:MF_01316}.
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DR   EMBL; AJ400848; CAB88709.1; -; Genomic_DNA.
DR   PIR; S02002; S02002.
DR   RefSeq; NP_054916.1; NC_002202.1.
DR   PDB; 3JCU; EM; 3.20 A; I/i=1-36.
DR   PDBsum; 3JCU; -.
DR   AlphaFoldDB; P62103; -.
DR   SMR; P62103; -.
DR   DIP; DIP-62015N; -.
DR   IntAct; P62103; 1.
DR   STRING; 3562.P62103; -.
DR   GeneID; 2715614; -.
DR   KEGG; soe:2715614; -.
DR   OrthoDB; 1641960at2759; -.
DR   Proteomes; UP000054095; Chloroplast.
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:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01316; PSII_PsbI; 1.
DR   InterPro; IPR003686; PSII_PsbI.
DR   InterPro; IPR037271; PSII_PsbI_sf.
DR   PANTHER; PTHR35772; PTHR35772; 1.
DR   Pfam; PF02532; PsbI; 1.
DR   SUPFAM; SSF161041; SSF161041; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Direct protein sequencing; Formylation;
KW   Membrane; Photosynthesis; Photosystem II; Plastid; Reaction center;
KW   Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..36
FT                   /note="Photosystem II reaction center protein I"
FT                   /id="PRO_0000219656"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01316"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:9632665"
FT   HELIX           2..24
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:3JCU"
SQ   SEQUENCE   36 AA;  4168 MW;  6B6C7FCB57BB6236 CRC64;
     MLTLKLFVYT VVIFFVSLFI FGFLSNDPGR NPGREE
 
 
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