PSBH_SPIOL
ID PSBH_SPIOL Reviewed; 73 AA.
AC P05146; Q9M3K3;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 115.
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, ECO:0000303|PubMed:2834086};
GN Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752};
OS Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
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 [GENOMIC DNA].
RX PubMed=2834086; DOI=10.1007/bf00420602;
RA Westhoff P., Farchaus J.W., Herrmann R.G.;
RT "The gene for the Mr 10,000 phosphoprotein associated with photosystem II
RT is part of the psbB operon of the spinach plastid chromosome.";
RL Curr. Genet. 11:165-169(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-11, SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-3, AND TOPOLOGY.
RA Michel H.P., Bennett J.;
RT "Identification of the phosphorylation site of an 8.3 kDa protein from
RT photosystem II of spinach.";
RL FEBS Lett. 212:103-108(1987).
RN [4]
RP PROTEIN SEQUENCE OF 2-11, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=2644131; DOI=10.1016/0014-5793(89)80482-x;
RA Ikeuchi M., Takio K., Inoue Y.;
RT "N-terminal sequencing of photosystem II low-molecular-mass proteins. 5 and
RT 4.1 kDa components of the O2-evolving core complex from higher plants.";
RL FEBS Lett. 242:263-269(1989).
RN [5]
RP PROTEIN SEQUENCE OF 2-10, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=3947072; DOI=10.1016/0003-9861(86)90097-4;
RA Farchaus J., Dilley R.A.;
RT "Purification and partial sequence of the Mr 10,000 phosphoprotein from
RT spinach thylakoids.";
RL Arch. Biochem. Biophys. 244:94-101(1986).
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, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes. {ECO:0000269|PubMed:2644131, ECO:0000269|PubMed:3947072,
CC ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|PubMed:2644131,
CC ECO:0000269|PubMed:3947072, ECO:0000269|Ref.3}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- PTM: Phosphorylation is a light-dependent reaction catalyzed by a
CC membrane-bound kinase (Ref.3). Phosphorylation occurs on Thr residue(s)
CC in the N-terminus of the protein. {ECO:0000255|HAMAP-Rule:MF_00752,
CC ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88756.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X07106; CAA30127.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88756.1; ALT_INIT; Genomic_DNA.
DR PIR; S00410; S00410.
DR RefSeq; NP_054963.1; NC_002202.1.
DR PDB; 3JCU; EM; 3.20 A; H/h=1-73.
DR PDBsum; 3JCU; -.
DR AlphaFoldDB; P05146; -.
DR SMR; P05146; -.
DR DIP; DIP-62014N; -.
DR IntAct; P05146; 1.
DR STRING; 3562.P05146; -.
DR GeneID; 2715613; -.
DR KEGG; soe:2715613; -.
DR OrthoDB; 1583583at2759; -.
DR Proteomes; UP000054095; Chloroplast.
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; Direct protein sequencing; Membrane;
KW Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2644131,
FT ECO:0000269|PubMed:3947072, ECO:0000269|Ref.3"
FT CHAIN 2..73
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000070537"
FT TOPO_DOM 2..40
FT /note="Stromal"
FT /evidence="ECO:0000269|Ref.3"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT TOPO_DOM 62..73
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752,
FT ECO:0000269|Ref.3"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT CONFLICT 29
FT /note="E -> K (in Ref. 1; CAA30127)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="G -> R (in Ref. 1; CAA30127)"
FT /evidence="ECO:0000305"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:3JCU"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:3JCU"
FT HELIX 40..61
FT /evidence="ECO:0007829|PDB:3JCU"
SQ SEQUENCE 73 AA; 7730 MW; 231EB9CA80DB05BE CRC64;
MATQTVESSS RSRPKPTTVG ALLKPLNSEY GKVAPGWGTT PLMGVAMALF AVFLSIILEI
YNSSVLLDGI SMN
