PSBH_THEVL
ID PSBH_THEVL Reviewed; 65 AA.
AC P19052; D0VWR6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 81.
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 Flags: Fragment;
GN Name=psbH {ECO:0000255|HAMAP-Rule:MF_00752};
OS Thermostichus vulcanus (Synechococcus vulcanus).
OC Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX NCBI_TaxID=32053;
RN [1]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=2493396; DOI=10.1016/0014-5793(89)80570-8;
RA Koike H., Mamada K., Ikeuchi M., Inoue Y.;
RT "Low-molecular-mass proteins in cyanobacterial photosystem II:
RT identification of psbH and psbK gene products by N-terminal sequencing.";
RL FEBS Lett. 244:391-396(1989).
RN [2]
RP PROTEIN SEQUENCE OF 1-9, COMPOSITION OF PHOTOSYSTEM II, AND SUBUNIT.
RX PubMed=12461137; DOI=10.1093/pcp/pcf168;
RA Kashino Y., Koike H., Yoshio M., Egashira H., Ikeuchi M., Pakrasi H.B.,
RA Satoh K.;
RT "Low-molecular-mass polypeptide components of a photosystem II preparation
RT from the thermophilic cyanobacterium Thermosynechococcus vulcanus.";
RL Plant Cell Physiol. 43:1366-1373(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12518057; DOI=10.1073/pnas.0135651100;
RA Kamiya N., Shen J.-R.;
RT "Crystal structure of oxygen-evolving photosystem II from
RT Thermosynechococcus vulcanus at 3.7-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:98-103(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 1-64 IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19433803; DOI=10.1073/pnas.0812797106;
RA Kawakami K., Umena Y., Kamiya N., Shen J.R.;
RT "Location of chloride and its possible functions in oxygen-evolving
RT photosystem II revealed by X-ray crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8567-8572(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21499260; DOI=10.1038/nature09913;
RA Umena Y., Kawakami K., Shen J.R., Kamiya N.;
RT "Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9
RT A.";
RL Nature 473:55-60(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-63 IN PHOTOSYSTEM II, FUNCTION,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23426624; DOI=10.1073/pnas.1219922110;
RA Koua F.H., Umena Y., Kawakami K., Shen J.R.;
RT "Structure of Sr-substituted photosystem II at 2.1 A resolution and its
RT implications in the mechanism of water oxidation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3889-3894(2013).
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, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:23426624}.
CC -!- COFACTOR:
CC Note=PSII binds multiple chlorophylls, carotenoids and specific lipids.
CC {ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803,
CC ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624};
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:12461137, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00752, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00752, ECO:0000269|PubMed:12518057,
CC ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC ECO:0000269|PubMed:23426624}.
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 PDB; 3A0B; X-ray; 3.70 A; H/h=1-64.
DR PDB; 3A0H; X-ray; 4.00 A; H/h=1-64.
DR PDB; 3WU2; X-ray; 1.90 A; H/h=1-63.
DR PDB; 4IL6; X-ray; 2.10 A; H/h=1-63.
DR PDB; 4UB6; X-ray; 1.95 A; H/h=1-65.
DR PDB; 4UB8; X-ray; 1.95 A; H/h=1-65.
DR PDB; 5B5E; X-ray; 1.87 A; H/h=1-65.
DR PDB; 5B66; X-ray; 1.85 A; H/h=1-65.
DR PDB; 5GTH; X-ray; 2.50 A; H/h=1-65.
DR PDB; 5GTI; X-ray; 2.50 A; H/h=1-65.
DR PDB; 5V2C; X-ray; 1.90 A; H/h=1-65.
DR PDB; 5WS5; X-ray; 2.35 A; H/h=1-65.
DR PDB; 5WS6; X-ray; 2.35 A; H/h=1-65.
DR PDB; 6JLJ; X-ray; 2.15 A; H/h=1-65.
DR PDB; 6JLK; X-ray; 2.15 A; H/h=1-65.
DR PDB; 6JLL; X-ray; 2.15 A; H/h=1-65.
DR PDB; 6JLM; X-ray; 2.35 A; H/h=1-65.
DR PDB; 6JLN; X-ray; 2.40 A; H/h=1-65.
DR PDB; 6JLO; X-ray; 2.40 A; H/h=1-65.
DR PDB; 6JLP; X-ray; 2.50 A; H/h=1-65.
DR PDB; 7CJI; X-ray; 2.35 A; H/h=1-65.
DR PDB; 7CJJ; X-ray; 2.40 A; H/h=1-65.
DR PDB; 7COU; X-ray; 2.25 A; H/h=1-65.
DR PDB; 7CZL; EM; 3.78 A; H/h=1-62.
DR PDB; 7D1T; EM; 1.95 A; H/h=1-63.
DR PDB; 7D1U; EM; 2.08 A; H/h=1-63.
DR PDB; 7DXA; EM; 3.14 A; h=1-65.
DR PDB; 7DXH; EM; 3.14 A; h=1-65.
DR PDB; 7EDA; EM; 2.78 A; H=1-62.
DR PDBsum; 3A0B; -.
DR PDBsum; 3A0H; -.
DR PDBsum; 3WU2; -.
DR PDBsum; 4IL6; -.
DR PDBsum; 4UB6; -.
DR PDBsum; 4UB8; -.
DR PDBsum; 5B5E; -.
DR PDBsum; 5B66; -.
DR PDBsum; 5GTH; -.
DR PDBsum; 5GTI; -.
DR PDBsum; 5V2C; -.
DR PDBsum; 5WS5; -.
DR PDBsum; 5WS6; -.
DR PDBsum; 6JLJ; -.
DR PDBsum; 6JLK; -.
DR PDBsum; 6JLL; -.
DR PDBsum; 6JLM; -.
DR PDBsum; 6JLN; -.
DR PDBsum; 6JLO; -.
DR PDBsum; 6JLP; -.
DR PDBsum; 7CJI; -.
DR PDBsum; 7CJJ; -.
DR PDBsum; 7COU; -.
DR PDBsum; 7CZL; -.
DR PDBsum; 7D1T; -.
DR PDBsum; 7D1U; -.
DR PDBsum; 7DXA; -.
DR PDBsum; 7DXH; -.
DR PDBsum; 7EDA; -.
DR AlphaFoldDB; P19052; -.
DR SMR; P19052; -.
DR DIP; DIP-48867N; -.
DR IntAct; P19052; 1.
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:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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; Photosynthesis;
KW Photosystem II; Thylakoid; Transmembrane; Transmembrane helix.
FT CHAIN <1..65
FT /note="Photosystem II reaction center protein H"
FT /id="PRO_0000070549"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TRANSMEM 29..44
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:21499260"
FT TOPO_DOM 45..65
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:21499260"
FT NON_TER 1
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:5B66"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:7DXA"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:5B66"
FT HELIX 27..48
FT /evidence="ECO:0007829|PDB:5B66"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5B66"
SQ SEQUENCE 65 AA; 7223 MW; A733182CBFD5841D CRC64;
ARRTWLGDIL RPLNSEYGKV APGWGTTPLM AVFMGLFLVF LLIILEIYNS TLILDGVNVS
WKALG
