PSBH_CHLRE
ID PSBH_CHLRE Reviewed; 88 AA.
AC P22666; B7U1H1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
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 8 kDa phosphoprotein {ECO:0000303|Ref.4};
GN Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=137c / CC-125;
RX PubMed=8343600; DOI=10.1007/bf00047405;
RA Johnson C.H., Schmidt G.W.;
RT "The psbB gene cluster of the Chlamydomonas reinhardtii chloroplast:
RT sequence and transcriptional analyses of psbN and psbH.";
RL Plant Mol. Biol. 22:645-658(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cw15;
RA O'Connor H.E., Nugent J.H., Purton S.;
RT "Characterisation of the Chlamydomonas reinhardtii psbH gene encoding the
RT 9.3 kDa phosphoprotein of photosystem II.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [4]
RP PROTEIN SEQUENCE OF 2-43, PHOSPHORYLATION AT THR-3, AND SUBCELLULAR
RP LOCATION.
RA Dedner N., Meyer H.E., Ashton C., Wildner G.F.;
RT "N-terminal sequence analysis of the 8 kDa protein in Chlamydomonas
RT reinhardii. Localization of the phosphothreonine.";
RL FEBS Lett. 236:77-82(1988).
RN [5]
RP SUBUNIT, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=1885590; DOI=10.1016/s0021-9258(18)55345-x;
RA de Vitry C., Diner B.A., Popo J.-L.;
RT "Photosystem II particles from Chlamydomonas reinhardtii. Purification,
RT molecular weight, small subunit composition, and protein phosphorylation.";
RL J. Biol. Chem. 266:16614-16621(1991).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=137c / CC-125;
RX PubMed=9112780; DOI=10.1104/pp.113.4.1359;
RA Summer E.J., Schmid V.H., Bruns B.U., Schmidt G.W.;
RT "Requirement for the H phosphoprotein in photosystem II of Chlamydomonas
RT reinhardtii.";
RL Plant Physiol. 113:1359-1368(1997).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-3.
RC STRAIN=2137;
RX PubMed=9554956; DOI=10.1016/s0005-2728(98)00013-9;
RA O'Connor H.E., Ruffle S.V., Cain A.J., Deak Z., Vass I., Nugent J.H.,
RA Purton S.;
RT "The 9-kDa phosphoprotein of photosystem II. Generation and
RT characterisation of Chlamydomonas mutants lacking PSII-H and a site-
RT directed mutant lacking the phosphorylation site.";
RL Biochim. Biophys. Acta 1364:63-72(1998).
RN [8]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
CC -!- FUNCTION: One of the components of the core complex of photosystem II
CC (PSII), required for its stability and/or assembly, possibly playing a
CC role in dimerization (PubMed:9112780, PubMed:9554956). 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, ECO:0000269|PubMed:9112780,
CC ECO:0000269|PubMed:9554956}.
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 PsbW, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the
CC oxygen-evolving complex and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000269|PubMed:1885590,
CC ECO:0000269|PubMed:9112780}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|PubMed:1885590,
CC ECO:0000269|PubMed:9112780, ECO:0000269|Ref.4}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000305|PubMed:9112780}.
CC -!- INDUCTION: A monocistronic transcript that is strongly expressed.
CC {ECO:0000269|PubMed:9112780}.
CC -!- PTM: Phosphorylation is a light-dependent reaction catalyzed by a
CC membrane-bound kinase (Ref.4). In vitro phosphorylation is incomplete
CC (PubMed:1885590). {ECO:0000269|PubMed:1885590, ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Loss of photosynthetic growth, cells grow
CC normally on a reduced carbon source. While all other PSII subunits are
CC synthesized and are inserted into thylakoids, they do not accumulate.
CC {ECO:0000269|PubMed:9112780, ECO:0000269|PubMed:9554956}.
CC -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
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DR EMBL; L13303; AAA02861.1; -; Genomic_DNA.
DR EMBL; Z15133; CAA78836.1; -; Genomic_DNA.
DR EMBL; Z23260; CAA80782.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50118.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00930.1; -; Genomic_DNA.
DR PIR; S01125; S01125.
DR PIR; S35147; S35147.
DR RefSeq; NP_958385.1; NC_005353.1.
DR PDB; 6KAC; EM; 2.70 A; H/h=1-88.
DR PDB; 6KAD; EM; 3.40 A; H/h=1-88.
DR PDB; 6KAF; EM; 3.73 A; H/h=1-88.
DR PDBsum; 6KAC; -.
DR PDBsum; 6KAD; -.
DR PDBsum; 6KAF; -.
DR AlphaFoldDB; P22666; -.
DR SMR; P22666; -.
DR STRING; 3055.DAA00930; -.
DR PaxDb; P22666; -.
DR PRIDE; P22666; -.
DR GeneID; 2717030; -.
DR KEGG; cre:ChreCp029; -.
DR eggNOG; ENOG502S8Y7; Eukaryota.
DR HOGENOM; CLU_190203_0_0_1; -.
DR InParanoid; P22666; -.
DR OrthoDB; 1583583at2759; -.
DR BioCyc; MetaCyc:CHRECP029-MON; -.
DR Proteomes; UP000006906; 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|Ref.4"
FT CHAIN 2..88
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000070502"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|Ref.4"
FT MUTAGEN 3
FT /note="T->A: No visible phenotype."
FT /evidence="ECO:0000269|PubMed:9554956"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6KAC"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6KAC"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 47..68
FT /evidence="ECO:0007829|PDB:6KAC"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:6KAC"
SQ SEQUENCE 88 AA; 9439 MW; 11CF2B710DB9062E CRC64;
MATGTSKAKP SKVNSDFQEP GLVTPLGTLL RPLNSEAGKV LPGWGTTVLM AVFILLFAAF
LLIILEIYNS SLILDDVSMS WETLAKVS
