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PSBO_SPIOL
ID   PSBO_SPIOL              Reviewed;         332 AA.
AC   P12359;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Oxygen-evolving enhancer protein 1, chloroplastic;
DE            Short=OEE1;
DE   AltName: Full=33 kDa subunit of oxygen evolving system of photosystem II;
DE   AltName: Full=33 kDa thylakoid membrane protein;
DE   AltName: Full=OEC 33 kDa subunit;
DE   Flags: Precursor;
GN   Name=PSBO;
OS   Spinacia oleracea (Spinach).
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 [MRNA].
RA   Tyagi A., Hermans J., Steppuhn R.C.J., Jansson C., Vater F., Herrmann R.G.;
RT   "Nucleotide sequence of cDNA clones encoding the complete '33 kDa'
RT   precursor protein associated with the photosynthetic oxygen-evolving
RT   complex from spinach.";
RL   Mol. Gen. Genet. 207:288-293(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 85-332.
RA   Oh-Oka H., Tanaka S., Wada K., Kuwabara T., Murata N.;
RT   "Complete amino acid sequence of 33 kDa protein isolated from spinach
RT   photosystem II particles.";
RL   FEBS Lett. 197:63-66(1986).
RN   [3]
RP   PROTEIN SEQUENCE OF 85-121.
RA   Yamamoto Y., Hermodson M.A., Krogmann D.W.;
RT   "Improved purification and N-terminal sequence of the 33-kDa protein in
RT   spinach PS II.";
RL   FEBS Lett. 195:155-158(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 85-91, SUBCELLULAR LOCATION, AND CHARACTERIZATION.
RX   PubMed=14736920; DOI=10.1073/pnas.0308164100;
RA   Spetea C., Hundal T., Lundin B., Heddad M., Adamska I., Andersson B.;
RT   "Multiple evidence for nucleotide metabolism in the chloroplast thylakoid
RT   lumen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:1409-1414(2004).
CC   -!- FUNCTION: Stabilizes the manganese cluster which is the primary site of
CC       water splitting (By similarity). Binds GTP after preillumination of
CC       photosystem II core complex. This binding is inhibited by DCMU.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:14736920}. Note=Associated with the photosystem II
CC       complex.
CC   -!- SIMILARITY: Belongs to the PsbO family. {ECO:0000305}.
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DR   EMBL; X05548; CAA29062.1; -; mRNA.
DR   PIR; A23613; A23613.
DR   PIR; S00415; S00415.
DR   PDB; 3JCU; EM; 3.20 A; O/o=1-332.
DR   PDBsum; 3JCU; -.
DR   AlphaFoldDB; P12359; -.
DR   SMR; P12359; -.
DR   DIP; DIP-62020N; -.
DR   IntAct; P12359; 1.
DR   PRIDE; P12359; -.
DR   GO; GO:0030095; C:chloroplast photosystem II; IDA:CAFA.
DR   GO; GO:0009654; C:photosystem II oxygen evolving complex; IMP:CAFA.
DR   GO; GO:0010242; F:oxygen evolving activity; IMP:CAFA.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IMP:CAFA.
DR   GO; GO:0010207; P:photosystem II assembly; IMP:CAFA.
DR   GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR   DisProt; DP00188; -.
DR   InterPro; IPR011250; OMP/PagP_b-brl.
DR   InterPro; IPR002628; PSII_MSP.
DR   PANTHER; PTHR34058; PTHR34058; 1.
DR   Pfam; PF01716; MSP; 1.
DR   SUPFAM; SSF56925; SSF56925; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Direct protein sequencing; Manganese; Membrane;
KW   Photosynthesis; Photosystem II; Plastid; Thylakoid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT   TRANSIT         ?..84
FT                   /note="Thylakoid"
FT   CHAIN           85..332
FT                   /note="Oxygen-evolving enhancer protein 1, chloroplastic"
FT                   /id="PRO_0000029561"
FT   CONFLICT        96
FT                   /note="Q -> N (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="Q -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="D -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           92..97
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   HELIX           100..103
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          136..144
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          194..200
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          206..212
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          217..220
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   HELIX           222..224
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          225..231
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          245..253
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   HELIX           258..263
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          279..290
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   TURN            292..294
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          296..302
FT                   /evidence="ECO:0007829|PDB:3JCU"
FT   STRAND          318..328
FT                   /evidence="ECO:0007829|PDB:3JCU"
SQ   SEQUENCE   332 AA;  35171 MW;  B15507F5835117FF CRC64;
     MAASLQASTT FLQPTKVASR NTLQLRSTQN VCKAFGVESA SSGGRLSLSL QSDLKELANK
     CVDATKLAGL ALATSALIAS GANAEGGKRL TYDEIQSKTY LEVKGTGTAN QCPTVEGGVD
     SFAFKPGKYT AKKFCLEPTK FAVKAEGISK NSGPDFQNTK LMTRLTYTLD EIEGPFEVSS
     DGTVKFEEKD GIDYAAVTVQ LPGGERVPFL FTIKQLVASG KPESFSGDFL VPSYRGSSFL
     DPKGRGGSTG YDNAVALPAG GRGDEEELQK ENNKNVASSK GTITLSVTSS KPETGEVIGV
     FQSLQPSDTD LGAKVPKDVK IEGVWYAQLE QQ
 
 
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