ID   PSBH_KLEBI              Reviewed;          79 AA.
AC   Q71KN4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 64.
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   Klebsormidium bilatum (Filamentous green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC   Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX   NCBI_TaxID=201239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lee J., Manhart J.R.;
RT   "psbB gene cluster in Charophyceae.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF482500; AAQ05924.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q71KN4; -.
DR   SMR; Q71KN4; -.
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..79
FT                   /note="Photosystem II reaction center protein H"
FT                   /id="PRO_0000070513"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
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   79 AA;  8451 MW;  FEED780C8459D992 CRC64;
     MATKTLDQDP NKQRPGAAVS SVLKPLNAEY GKVAPGWGTT VLMGVFMALF AVFLVIILEL
     YNASVLLDGV PVSWQSVQS