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PSBS_SPIOL
ID   PSBS_SPIOL              Reviewed;         274 AA.
AC   Q02060;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Photosystem II 22 kDa protein, chloroplastic;
DE   AltName: Full=CP22;
DE   Flags: Precursor;
GN   Name=PSBS;
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].
RC   STRAIN=cv. Monatol; TISSUE=Leaf;
RX   PubMed=1360412; DOI=10.1016/0014-5793(92)81462-u;
RA   Wedel N., Klein R., Ljungberg U., Andersson B., Herrmann R.G.;
RT   "The single-copy gene psbS codes for a phylogenetically intriguing 22 kDa
RT   polypeptide of photosystem II.";
RL   FEBS Lett. 314:61-66(1992).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1451805; DOI=10.1016/0014-5793(92)81463-v;
RA   Kim S., Sandusky P., Bowlby N.R., Aebersold R., Green B.R., Vlahakis S.,
RA   Yocum C.F., Pichersky E.;
RT   "Characterization of a spinach psbS cDNA encoding the 22 kDa protein of
RT   photosystem II.";
RL   FEBS Lett. 314:67-71(1992).
CC   -!- FUNCTION: Seems to be involved in non-photochemical quenching, a
CC       process maintains the balance between dissipation and utilization of
CC       light energy to minimize generation of oxidizing molecules, thereby
CC       protecting the plant against photo-oxidative damage. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q02060; Q02060: PSBS; NbExp=3; IntAct=EBI-16169411, EBI-16169411;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC       pass membrane protein. Note=Extreme lateral location to the appressed
CC       thylakoid regions.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the ELIP/psbS family. {ECO:0000305}.
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DR   EMBL; S49864; AAB24338.1; -; mRNA.
DR   EMBL; X68552; CAA48557.1; -; mRNA.
DR   PIR; S26953; S26953.
DR   PDB; 4RI2; X-ray; 2.35 A; A/B=63-274.
DR   PDB; 4RI3; X-ray; 2.70 A; A/B=63-274.
DR   PDBsum; 4RI2; -.
DR   PDBsum; 4RI3; -.
DR   AlphaFoldDB; Q02060; -.
DR   SMR; Q02060; -.
DR   DIP; DIP-61707N; -.
DR   PRIDE; Q02060; -.
DR   OrthoDB; 1327341at2759; -.
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:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0051219; F:phosphoprotein binding; IPI:CAFA.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   InterPro; IPR022796; Chloroa_b-bind.
DR   Pfam; PF00504; Chloroa_b-bind; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Membrane; Photosynthesis; Photosystem II;
KW   Plastid; Repeat; Thylakoid; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..69
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           70..274
FT                   /note="Photosystem II 22 kDa protein, chloroplastic"
FT                   /id="PRO_0000007808"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          64..167
FT                   /note="1"
FT   REPEAT          168..273
FT                   /note="2"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:4RI3"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   HELIX           96..120
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   HELIX           124..127
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   HELIX           141..154
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   HELIX           200..224
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   HELIX           228..236
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   HELIX           240..259
FT                   /evidence="ECO:0007829|PDB:4RI2"
FT   STRAND          263..267
FT                   /evidence="ECO:0007829|PDB:4RI2"
SQ   SEQUENCE   274 AA;  29197 MW;  6FC3FF7EF648DCD4 CRC64;
     MAQAMLLMMP GVSTTNTIDL KRNALLKLQI QKIKPKSSTS NLFFSPLPSS SSSSSTVFKT
     LALFKSKAKA PKKVEKPKLK VEDGLFGTSG GIGFTKENEL FVGRVAMIGF AASLLGEGIT
     GKGILSQLNL ETGIPIYEAE PLLLFFILFT LLGAIGALGD RGRFVDEPTT GLEKAVIPPG
     KDVRSALGLK TKGPLFGFTK SNELFVGRLA QLGFAFSLIG EIITGKGALA QLNIETGVPI
     NEIEPLVLLN VVFFFIAAIN PGTGKFITDD EEED
 
 
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