ID   PSBH_LIRTU              Reviewed;          73 AA.
AC   Q0G9J0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 53.
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   Liriodendron tulipifera (Tuliptree) (Tulip poplar).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Magnoliaceae;
OC   Liriodendron.
OX   NCBI_TaxID=3415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17020608; DOI=10.1186/1471-2148-6-77;
RA   Cai Z., Penaflor C., Kuehl J.V., Leebens-Mack J., Carlson J.E.,
RA   dePamphilis C.W., Boore J.L., Jansen R.K.;
RT   "Complete plastid genome sequences of Drimys, Liriodendron, and Piper:
RT   implications for the phylogenetic relationships of magnoliids.";
RL   BMC Evol. Biol. 6:77-77(2006).
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}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00752}.
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; DQ899947; ABI32538.1; -; Genomic_DNA.
DR   RefSeq; YP_740231.1; NC_008326.1.
DR   AlphaFoldDB; Q0G9J0; -.
DR   SMR; Q0G9J0; -.
DR   GeneID; 4266655; -.
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   3: Inferred from homology;
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_0000275760"
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..16
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"
SQ   SEQUENCE   73 AA;  7767 MW;  1863800E8CC30535 CRC64;
     MATQTVEGSS RSGPRRTITG DLLKPLNSEY GKVAPGWGTT PFMGVAMALF AIFLSIILEI
     YNSSVLLDGI SMS