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PSBH_HORVU
ID   PSBH_HORVU              Reviewed;          73 AA.
AC   P12363; A1E9L9;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Photosystem II reaction center protein H {ECO:0000255|HAMAP-Rule:MF_00752};
DE            Short=PSII-H {ECO:0000255|HAMAP-Rule:MF_00752};
DE   AltName: Full=Photosystem II 10 kDa phosphoprotein {ECO:0000255|HAMAP-Rule:MF_00752};
GN   Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752};
OS   Hordeum vulgare (Barley).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Sabarlis;
RX   PubMed=2654887; DOI=10.1093/nar/17.7.2859;
RA   Andreeva A.V., Buryakova A.A., Reverdatto S.V., Chakhmakhcheva O.G.,
RA   Efimov V.A.;
RT   "Nucleotide sequence of the 5.2 kbp barley chloroplast DNA fragment,
RT   containing psbB-psbH-petB-petD gene cluster.";
RL   Nucleic Acids Res. 17:2859-2860(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Sabarlis;
RX   PubMed=1804121;
RA   Efimov V.A., Andreeva A.V., Reverdatto S.V., Chakhmakhcheva O.G.;
RT   "Photosystem II of rye. Nucleotide sequence of the psbB, psbC, psbE, psbF,
RT   psbH genes of rye and chloroplast DNA regions adjacent to them.";
RL   Bioorg. Khim. 17:1369-1385(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex;
RX   PubMed=17534593; DOI=10.1007/s00122-007-0567-4;
RA   Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H.,
RA   Tomkins J., Rognli O.A., Daniell H., Clarke J.L.;
RT   "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor
RT   and Agrostis stolonifera, and comparative analyses with other grass
RT   genomes.";
RL   Theor. Appl. Genet. 115:571-590(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Steffi;
RX   PubMed=19137553; DOI=10.1002/pmic.200800337;
RA   Ploescher M., Granvogl B., Zoryan M., Reisinger V., Eichacker L.A.;
RT   "Mass spectrometric characterization of membrane integral low molecular
RT   weight proteins from photosystem II in barley etioplasts.";
RL   Proteomics 9:625-635(2009).
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_00752}.
CC   -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC       PsbB, PsbC, PsbD, numerous small proteins, at least 3 peripheral
CC       proteins of the oxygen-evolving complex and a large number of
CC       cofactors. It forms dimeric complexes (By similarity). Detected in both
CC       etioplasts and green leaves; PSII is only assembled in green leaves
CC       (PubMed:19137553). {ECO:0000255|HAMAP-Rule:MF_00752,
CC       ECO:0000269|PubMed:19137553}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000305|PubMed:19137553}; Single-
CC       pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00752,
CC       ECO:0000305|PubMed:19137553}.
CC   -!- PTM: Phosphorylation is a light-dependent reaction catalyzed by a
CC       membrane-bound kinase; phosphorylation occurs on Thr residue(s) in the
CC       N-terminus of the protein. {ECO:0000255|HAMAP-Rule:MF_00752}.
CC   -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00752}.
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DR   EMBL; X14107; CAA32265.1; -; Genomic_DNA.
DR   EMBL; EF115541; ABK79440.1; -; Genomic_DNA.
DR   PIR; S04148; S04148.
DR   RefSeq; YP_874681.1; NC_008590.1.
DR   AlphaFoldDB; P12363; -.
DR   SMR; P12363; -.
DR   GeneID; 4525078; -.
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:0042301; F:phosphate ion binding; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0050821; P:protein stabilization; IEA:InterPro.
DR   Gene3D; 1.20.5.880; -; 1.
DR   HAMAP; MF_00752; PSII_PsbH; 1.
DR   InterPro; IPR001056; PSII_PsbH.
DR   InterPro; IPR036863; PSII_PsbH_sf.
DR   PANTHER; PTHR34469; PTHR34469; 1.
DR   Pfam; PF00737; PsbH; 1.
DR   SUPFAM; SSF161025; SSF161025; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Membrane; Phosphoprotein; Photosynthesis; Photosystem II;
KW   Plastid; Thylakoid; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..73
FT                   /note="Photosystem II reaction center protein H"
FT                   /id="PRO_0000070511"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT   MOD_RES         5
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
SQ   SEQUENCE   73 AA;  7801 MW;  9685856982237A41 CRC64;
     MATQTVEDSS KPRPKRTGAG SLLKPLNSEY GKVAPGWGTT PFMGVAMALF AIFLSIILEI
     YNSSILLDGI LTN
 
 
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