DINJ_ECOLI
ID DINJ_ECOLI Reviewed; 86 AA.
AC Q47150;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Antitoxin DinJ;
GN Name=dinJ; OrderedLocusNames=b0226, JW0216;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7596361; DOI=10.1016/0165-7992(95)90024-1;
RA Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.;
RT "dinP, a new gene in Escherichia coli, whose product shows similarities to
RT UmuC and its homologues.";
RL Mutat. Res. 347:1-7(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION AS AN ANTITOXIN, AND SUBUNIT.
RC STRAIN=K12 / BW25113;
RX PubMed=17263853; DOI=10.1111/j.1574-6968.2006.00563.x;
RA Motiejunaite R., Armalyte J., Markuckas A., Suziedeliene E.;
RT "Escherichia coli dinJ-yafQ genes act as a toxin-antitoxin module.";
RL FEMS Microbiol. Lett. 268:112-119(2007).
RN [6]
RP FUNCTION AS AN ANTITOXIN, CLEAVAGE BY LON AND CLPX PROTEASES, SUBUNIT,
RP DNA-BINDING, AND INDUCTION.
RC STRAIN=K12 / BW25113, and K12 / DH5-alpha;
RX PubMed=19210620; DOI=10.1111/j.1365-2958.2008.06572.x;
RA Prysak M.H., Mozdzierz C.J., Cook A.M., Zhu L., Zhang Y., Inouye M.,
RA Woychik N.A.;
RT "Bacterial toxin YafQ is an endoribonuclease that associates with the
RT ribosome and blocks translation elongation through sequence-specific and
RT frame-dependent mRNA cleavage.";
RL Mol. Microbiol. 71:1071-1087(2009).
RN [7]
RP FUNCTION IN BIOFILM FORMATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19707553; DOI=10.1371/journal.pone.0006785;
RA Kolodkin-Gal I., Verdiger R., Shlosberg-Fedida A., Engelberg-Kulka H.;
RT "A differential effect of E. coli toxin-antitoxin systems on cell death in
RT liquid media and biofilm formation.";
RL PLoS ONE 4:E6785-E6785(2009).
RN [8] {ECO:0007744|PDB:4Q2U}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION AS A REPRESSOR, SUBUNIT,
RP INDUCTION, DNA-BINDING, AND MUTAGENESIS OF 2-ALA--ASP-12; 2-ALA--GLU-44;
RP ARG-10 AND ARG-35.
RX PubMed=24898247; DOI=10.1074/jbc.m114.573006;
RA Ruangprasert A., Maehigashi T., Miles S.J., Giridharan N., Liu J.X.,
RA Dunham C.M.;
RT "Mechanisms of toxin inhibition and transcriptional repression by
RT Escherichia coli DinJ-YafQ.";
RL J. Biol. Chem. 289:20559-20569(2014).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system
CC (PubMed:17263853). A labile antitoxin that counteracts the effect of
CC cognate toxin YafQ (PubMed:17263853). YafQ and DinJ together bind their
CC own promoter, and repress its expression (PubMed:24898247). There are 2
CC operators with imperfect inverted repeats (IR) in the dinJ promoter,
CC YafQ-(DinJ)2-YafQ only binds to the first (most upstream) of them to
CC repress transcription; binding to a single IR is sufficient for
CC activity in vivo and in vitro (PubMed:24898247). DinJ alone is as
CC potent a transcriptional repressor as the heterotetramer and also only
CC needs to bind 1 IR to act (PubMed:24898247).
CC {ECO:0000269|PubMed:17263853, ECO:0000269|PubMed:24898247}.
CC -!- FUNCTION: Cell death governed by the MazE-MazF and DinJ-YafQ TA systems
CC seems to play a role in biofilm formation (PubMed:19707553).
CC {ECO:0000269|PubMed:19707553}.
CC -!- SUBUNIT: Forms a heterotetramer with antitoxin DinJ, with 2 YafQ-DinJ
CC dimers associated via the N-terminus of the DinJ antitoxins (YafQ-
CC (DinJ)2-YafQ) (PubMed:17263853, PubMed:24898247). In this complex the
CC toxin activity is inhibited. {ECO:0000269|PubMed:17263853,
CC ECO:0000269|PubMed:19210620, ECO:0000269|PubMed:24898247}.
CC -!- INDUCTION: Not induced by the DNA damaging agent mitomycin C
CC (PubMed:19210620). Transcription is autorepressed by DinJ or YafQ-
CC (DinJ)2-YafQ via operator 1, repressed by LexA via operator 2
CC (PubMed:24898247). {ECO:0000269|PubMed:19210620,
CC ECO:0000269|PubMed:24898247}.
CC -!- PTM: Probably degraded by the Lon and ClpPX proteases in vivo.
CC {ECO:0000269|PubMed:19210620}.
CC -!- DISRUPTION PHENOTYPE: Cells missing dinJ-yafQ have reduced biofilm
CC formation. {ECO:0000269|PubMed:19707553}.
CC -!- SIMILARITY: Belongs to the RelB/DinJ antitoxin family. {ECO:0000305}.
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DR EMBL; D38582; BAA07588.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73330.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77896.1; -; Genomic_DNA.
DR PIR; C64747; C64747.
DR RefSeq; NP_414761.1; NC_000913.3.
DR RefSeq; WP_000729703.1; NZ_SSZK01000029.1.
DR PDB; 4Q2U; X-ray; 1.80 A; A/C/E/G/I/K/M/O=1-86.
DR PDBsum; 4Q2U; -.
DR AlphaFoldDB; Q47150; -.
DR SMR; Q47150; -.
DR BioGRID; 4259772; 55.
DR BioGRID; 849313; 3.
DR ComplexPortal; CPX-1079; DinJ-YafQ toxin-antitoxin complex.
DR DIP; DIP-9446N; -.
DR IntAct; Q47150; 2.
DR STRING; 511145.b0226; -.
DR jPOST; Q47150; -.
DR PaxDb; Q47150; -.
DR PRIDE; Q47150; -.
DR EnsemblBacteria; AAC73330; AAC73330; b0226.
DR EnsemblBacteria; BAA77896; BAA77896; BAA77896.
DR GeneID; 944914; -.
DR KEGG; ecj:JW0216; -.
DR KEGG; eco:b0226; -.
DR PATRIC; fig|1411691.4.peg.2057; -.
DR EchoBASE; EB2936; -.
DR eggNOG; COG3077; Bacteria.
DR HOGENOM; CLU_154558_12_2_6; -.
DR OMA; FEVRIPN; -.
DR PhylomeDB; Q47150; -.
DR BioCyc; EcoCyc:G6110-MON; -.
DR BioCyc; MetaCyc:G6110-MON; -.
DR PRO; PR:Q47150; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000df0; -.
DR GO; GO:0110001; C:toxin-antitoxin complex; IPI:ComplexPortal.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0015643; F:toxic substance binding; IDA:EcoCyc.
DR GO; GO:2000143; P:negative regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR GO; GO:0044010; P:single-species biofilm formation; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.1220.10; -; 1.
DR InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR InterPro; IPR026262; DinJ.
DR InterPro; IPR007337; RelB/DinJ.
DR PANTHER; PTHR38781; PTHR38781; 1.
DR Pfam; PF04221; RelB; 1.
DR PIRSF; PIRSF003108; DinJ; 1.
DR TIGRFAMs; TIGR02384; RelB_DinJ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor;
KW Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..86
FT /note="Antitoxin DinJ"
FT /id="PRO_0000079903"
FT MUTAGEN 2..44
FT /note="Missing: About 50% loss of promoter repression,
FT probably forms YafQ-DinQ dimers."
FT /evidence="ECO:0000269|PubMed:24898247"
FT MUTAGEN 2..12
FT /note="Missing: About 75% loss of promoter repression,
FT probably forms YafQ-DinQ tetramers."
FT /evidence="ECO:0000269|PubMed:24898247"
FT MUTAGEN 10
FT /note="R->A: Nearly complete loss of promoter repression,
FT YafQ-(DinJ)2-YafQ no longer binds DNA."
FT /evidence="ECO:0000269|PubMed:24898247"
FT MUTAGEN 35
FT /note="R->A: About 90% loss of promoter repression, YafQ-
FT (DinJ)2-YafQ no longer binds DNA."
FT /evidence="ECO:0000269|PubMed:24898247"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:4Q2U"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4Q2U"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4Q2U"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:4Q2U"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:4Q2U"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4Q2U"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4Q2U"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:4Q2U"
SQ SEQUENCE 86 AA; 9406 MW; 9B8786E70D90B3E2 CRC64;
MAANAFVRAR IDEDLKNQAA DVLAGMGLTI SDLVRITLTK VAREKALPFD LREPNQLTIQ
SIKNSEAGID VHKAKDADDL FDKLGI
