PSBH_PEA
ID PSBH_PEA Reviewed; 73 AA.
AC Q9XQR3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 79.
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};
DE AltName: Full=Photosystem II 9 kDa phosphoprotein {ECO:0000303|Ref.2};
GN Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752};
OS Pisum sativum (Garden pea).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lehmbeck J., Stummann B.M., Henningsen K.W.;
RT "Nucleotide sequence of the 5.6 kbp psbB operon of pea chloroplast DNA.";
RL Physiol. Plantarum 76:57-64(1989).
RN [2]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Feltham First;
RX DOI=10.1038/269344a0;
RA Bennett J.;
RT "Phosphorylation of chloroplast membrane polypeptides.";
RL Nature 269:344-346(1977).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|Ref.2}; Single-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000305|Ref.2}.
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; AF153442; AAD41887.1; -; Genomic_DNA.
DR PDB; 5XNL; EM; 2.70 A; H/h=1-73.
DR PDB; 5XNM; EM; 3.20 A; H/h=1-73.
DR PDB; 6YP7; EM; 3.80 A; H/h=13-72.
DR PDBsum; 5XNL; -.
DR PDBsum; 5XNM; -.
DR PDBsum; 6YP7; -.
DR AlphaFoldDB; Q9XQR3; -.
DR SMR; Q9XQR3; -.
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 3D-structure; Chloroplast; Membrane; Phosphoprotein; Photosynthesis;
KW Photosystem II; 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_0000070526"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
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"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:5XNL"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:5XNL"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:5XNL"
FT HELIX 40..61
FT /evidence="ECO:0007829|PDB:5XNL"
SQ SEQUENCE 73 AA; 7858 MW; 238F563680B8B56C CRC64;
MATQTVENSS RSGPRRTAVG DLLKPLNSEY GKVAPGWGTT PLMGIAMALF AVFLSIILEI
YNSSLLLDQI SMN
