PSBH_SYNY3
ID PSBH_SYNY3 Reviewed; 64 AA.
AC P14835;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
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=6 kDa phosphoprotein {ECO:0000303|PubMed:8495743};
GN Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752}; OrderedLocusNames=ssl2598;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=2106663; DOI=10.1093/nar/18.1.194;
RA Mayes S.R., Barber J.;
RT "Nucleotide sequence of the psbH gene of the cyanobacterium Synechocystis
RT 6803.";
RL Nucleic Acids Res. 18:194-194(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=2129396; DOI=10.1007/bf00028780;
RA Abdel-Mawgood A.L., Dilley R.A.;
RT "Cloning and nucleotide sequence of the psbH gene from cyanobacterium
RT Synechocystis 6803.";
RL Plant Mol. Biol. 14:445-446(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=1907512; DOI=10.1007/bf00039508;
RA Mayes S.R., Barber J.;
RT "Primary structure of the psbN-psbH-petC-petA gene cluster of the
RT cyanobacterium Synechocystis PCC 6803.";
RL Plant Mol. Biol. 17:289-293(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [5]
RP PROTEIN SEQUENCE OF 2-18, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=12069591; DOI=10.1021/bi026012+;
RA Kashino Y., Lauber W.M., Carroll J.A., Wang Q., Whitmarsh J., Satoh K.,
RA Pakrasi H.B.;
RT "Proteomic analysis of a highly active photosystem II preparation from the
RT cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel
RT polypeptides.";
RL Biochemistry 41:8004-8012(2002).
RN [6]
RP FUNCTION, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803-G;
RX DOI=10.1021/bi00057a008;
RA Mayes S.R., Dubbs J.M., Vass I., Hideg E., Nagy L., Barber J.;
RT "Further characterization of the psbH locus of Synechocystis sp. PCC 6803:
RT Inactivation of psbH impairs QA to QB electron transport in photosystem
RT 2.";
RL Biochemistry 32:1454-1465(1993).
RN [7]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8495743; DOI=10.1016/0014-5793(93)81443-4;
RA Race H.L., Gounaris K.;
RT "Identification of the psbH gene product as a 6 kDa phosphoprotein in the
RT cyanobacterium Synechocystis 6803.";
RL FEBS Lett. 323:35-39(1993).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803-G;
RX PubMed=7626631; DOI=10.1021/bi00029a040;
RA Komenda J., Barber J.;
RT "Comparison of psbO and psbH deletion mutants of Synechocystis PCC 6803
RT indicates that degradation of D1 protein is regulated by the QB site and
RT dependent on protein synthesis.";
RL Biochemistry 34:9625-9631(1995).
CC -!- FUNCTION: One of the components of the core complex of photosystem II
CC (PSII), required for its stability and/or assembly. May regulate
CC electron transport between the quinone binding sites of the reaction
CC center (PubMed:7626631, Ref.6). PSII is a light-driven
CC water:plastoquinone oxidoreductase that uses light energy to abstract
CC 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:7626631,
CC ECO:0000269|Ref.6}.
CC -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral
CC proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms
CC dimeric complexes. {ECO:0000255|HAMAP-Rule:MF_00752,
CC ECO:0000269|PubMed:12069591, ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00752, ECO:0000269|PubMed:12069591,
CC ECO:0000269|PubMed:8495743}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00752}.
CC -!- INDUCTION: A monocistronic transcript that is strongly expressed.
CC {ECO:0000269|Ref.6}.
CC -!- PTM: Phosphorylated in vitro in the presence or absence of light;
CC phosphorylation is inhibited by oxidizing conditions, DCMU and zinc
CC ions. {ECO:0000269|PubMed:8495743}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth under photoautotrophic conditions
CC and increased photosensitivity; approximately normal amounts of PSII
CC accumulate but electron flow from QA to QB is impaired (Ref.6).
CC Increased photodamage to D1 but it is degraded slower (PubMed:7626631).
CC {ECO:0000269|PubMed:7626631, ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the PsbH family. {ECO:0000255|HAMAP-
CC Rule:MF_00752}.
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DR EMBL; X17687; CAA35677.1; -; Genomic_DNA.
DR EMBL; X16394; CAA34430.1; -; Genomic_DNA.
DR EMBL; X58532; CAA41420.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17629.1; -; Genomic_DNA.
DR PIR; S07588; S07588.
DR PDB; 6WJ6; EM; 2.58 A; H=1-64.
DR PDB; 7N8O; EM; 1.93 A; H/h=1-64.
DR PDB; 7RCV; EM; 2.01 A; H/h=1-64.
DR PDBsum; 6WJ6; -.
DR PDBsum; 7N8O; -.
DR PDBsum; 7RCV; -.
DR AlphaFoldDB; P14835; -.
DR SMR; P14835; -.
DR IntAct; P14835; 6.
DR STRING; 1148.1652709; -.
DR PaxDb; P14835; -.
DR PRIDE; P14835; -.
DR EnsemblBacteria; BAA17629; BAA17629; BAA17629.
DR KEGG; syn:ssl2598; -.
DR eggNOG; ENOG50332MV; Bacteria.
DR InParanoid; P14835; -.
DR OMA; PLMAVFM; -.
DR PhylomeDB; P14835; -.
DR BioCyc; MetaCyc:PSBH-MON; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030096; C:plasma membrane-derived thylakoid photosystem II; IDA:UniProtKB.
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; Direct protein sequencing; Membrane; Phosphoprotein;
KW Photosynthesis; Photosystem II; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12069591"
FT CHAIN 2..64
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000070550"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00752"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:7N8O"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:7N8O"
FT HELIX 28..49
FT /evidence="ECO:0007829|PDB:7N8O"
SQ SEQUENCE 64 AA; 7116 MW; 5D056E24A56A121F CRC64;
MAQRTRLGDI LRPLNSEYGK VVPGWGTTPV MGVFMALFLV FLLIILQIYN SSLILEGFSV
DWAG
