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PSBJ_THEVL
ID   PSBJ_THEVL              Reviewed;          40 AA.
AC   Q7DGD4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Photosystem II reaction center protein J {ECO:0000255|HAMAP-Rule:MF_01305};
DE            Short=PSII-J {ECO:0000255|HAMAP-Rule:MF_01305};
GN   Name=psbJ {ECO:0000255|HAMAP-Rule:MF_01305};
OS   Thermostichus vulcanus (Synechococcus vulcanus).
OC   Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX   NCBI_TaxID=32053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) 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   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR, SUBUNIT,
RP   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   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4-40 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). PSII is a light-driven water:plastoquinone oxidoreductase that
CC       uses light energy to abstract electrons from H(2)O, generating O(2) and
CC       a proton gradient subsequently used for ATP formation. It consists of a
CC       core antenna complex that captures photons, and an electron transfer
CC       chain that converts photonic excitation into a charge separation.
CC       {ECO:0000255|HAMAP-Rule:MF_01305, 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:19433803, ECO:0000269|PubMed:21499260,
CC       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_01305,
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_01305, ECO:0000269|PubMed:19433803,
CC       ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Single-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01305,
CC       ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260,
CC       ECO:0000269|PubMed:23426624}.
CC   -!- SIMILARITY: Belongs to the PsbJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01305}.
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DR   EMBL; AB086860; BAC53637.1; -; Genomic_DNA.
DR   PDB; 3A0B; X-ray; 3.70 A; J/j=1-40.
DR   PDB; 3A0H; X-ray; 4.00 A; J/j=1-40.
DR   PDB; 3WU2; X-ray; 1.90 A; J/j=1-40.
DR   PDB; 4IL6; X-ray; 2.10 A; J/j=4-40.
DR   PDB; 4UB6; X-ray; 1.95 A; J/j=2-40.
DR   PDB; 4UB8; X-ray; 1.95 A; J/j=2-40.
DR   PDB; 5B5E; X-ray; 1.87 A; J/j=1-40.
DR   PDB; 5B66; X-ray; 1.85 A; J/j=1-40.
DR   PDB; 5GTH; X-ray; 2.50 A; J/j=2-40.
DR   PDB; 5GTI; X-ray; 2.50 A; J/j=2-40.
DR   PDB; 5V2C; X-ray; 1.90 A; J/j=1-40.
DR   PDB; 5WS5; X-ray; 2.35 A; J/j=2-40.
DR   PDB; 5WS6; X-ray; 2.35 A; J/j=2-40.
DR   PDB; 6JLJ; X-ray; 2.15 A; J/j=2-40.
DR   PDB; 6JLK; X-ray; 2.15 A; J/j=2-40.
DR   PDB; 6JLL; X-ray; 2.15 A; J/j=2-40.
DR   PDB; 6JLM; X-ray; 2.35 A; J/j=2-40.
DR   PDB; 6JLN; X-ray; 2.40 A; J/j=2-40.
DR   PDB; 6JLO; X-ray; 2.40 A; J/j=2-40.
DR   PDB; 6JLP; X-ray; 2.50 A; J/j=2-40.
DR   PDB; 7CJI; X-ray; 2.35 A; J/j=2-40.
DR   PDB; 7CJJ; X-ray; 2.40 A; J/j=2-40.
DR   PDB; 7COU; X-ray; 2.25 A; J/j=2-40.
DR   PDB; 7D1T; EM; 1.95 A; J/j=4-40.
DR   PDB; 7D1U; EM; 2.08 A; J/j=4-40.
DR   PDB; 7EDA; EM; 2.78 A; J=1-40.
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; 7D1T; -.
DR   PDBsum; 7D1U; -.
DR   PDBsum; 7EDA; -.
DR   AlphaFoldDB; Q7DGD4; -.
DR   SMR; Q7DGD4; -.
DR   DIP; DIP-48870N; -.
DR   IntAct; Q7DGD4; 1.
DR   EvolutionaryTrace; Q7DGD4; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01305; PSII_PsbJ; 1.
DR   InterPro; IPR002682; PSII_PsbJ.
DR   InterPro; IPR037267; PSII_PsbJ_sf.
DR   Pfam; PF01788; PsbJ; 1.
DR   SUPFAM; SSF161021; SSF161021; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Photosynthesis; Photosystem II; Reaction center;
KW   Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..40
FT                   /note="Photosystem II reaction center protein J"
FT                   /id="PRO_0000292241"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:21499260"
FT   TRANSMEM        12..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:21499260"
FT   TOPO_DOM        27..40
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:21499260"
FT   HELIX           10..32
FT                   /evidence="ECO:0007829|PDB:5B66"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:7D1T"
SQ   SEQUENCE   40 AA;  4105 MW;  4D05FAA8C690069E CRC64;
     MMSEGGRIPL WIVATVAGMG VIVIVGLFFY GAYAGLGSSL
 
 
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