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Protein

Antitoxin DinJ

Gene

dinJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antitoxin component of a toxin-antitoxin (TA) module. A labile antitoxin that counteracts the effect of the YafQ toxin. YafQ and DinJ together bind their own promoter, and by analogy to other TA modules probably repress its expression.
Cell death governed by the MazE-MazF and DinJ-YafQ TA modules seems to play a role in biofilm formation.

GO - Molecular functioni

  • bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding Source: EcoCyc
  • DNA binding Source: EcoCyc
  • toxic substance binding Source: EcoCyc

GO - Biological processi

  • negative regulation of DNA-templated transcription, initiation Source: EcoCyc
  • single-species biofilm formation Source: EcoCyc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6110-MONOMER.
ECOL316407:JW0216-MONOMER.
MetaCyc:G6110-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Antitoxin DinJ
Gene namesi
Name:dinJ
Ordered Locus Names:b0226, JW0216
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13142. dinJ.

Pathology & Biotechi

Disruption phenotypei

Cells missing dinJ-yafQ have reduced biofilm formation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8686Antitoxin DinJPRO_0000079903Add
BLAST

Post-translational modificationi

Probably degraded by the Lon and ClpPX proteases in vivo.

Proteomic databases

PaxDbiQ47150.
PRIDEiQ47150.

Expressioni

Inductioni

Not induced by the DNA damaging agent mitomycin C.1 Publication

Gene expression databases

CollecTFiEXPREG_00000df0.

Interactioni

Subunit structurei

Forms a complex with toxin YafQ, possibly a heterotetramer. In this complex the toxin activity is inhibited.2 Publications

Protein-protein interaction databases

BioGridi4259772. 55 interactions.
DIPiDIP-9446N.
IntActiQ47150. 2 interactions.
STRINGi511145.b0226.

Structurei

Secondary structure

1
86
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Helixi13 – 2412Combined sources
Turni25 – 273Combined sources
Helixi30 – 4415Combined sources
Helixi56 – 6712Combined sources
Turni68 – 703Combined sources
Beta strandi71 – 766Combined sources
Helixi77 – 848Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q2UX-ray1.80A/C/E/G/I/K/M/O1-86[»]
ProteinModelPortaliQ47150.
SMRiQ47150. Positions 3-86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RelB/DinJ antitoxin family.Curated

Phylogenomic databases

eggNOGiENOG4105QHH. Bacteria.
COG3077. LUCA.
HOGENOMiHOG000008424.
KOiK07473.
OMAiFEVRIPN.
OrthoDBiEOG6SJJS7.

Family and domain databases

InterProiIPR026262. DinJ.
IPR007337. RelB/DinJ.
[Graphical view]
PfamiPF04221. RelB. 1 hit.
[Graphical view]
PIRSFiPIRSF003108. DinJ. 1 hit.
TIGRFAMsiTIGR02384. RelB_DinJ. 1 hit.

Sequencei

Sequence statusi: Complete.

Q47150-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANAFVRAR IDEDLKNQAA DVLAGMGLTI SDLVRITLTK VAREKALPFD
60 70 80
LREPNQLTIQ SIKNSEAGID VHKAKDADDL FDKLGI
Length:86
Mass (Da):9,406
Last modified:November 1, 1997 - v1
Checksum:i9B8786E70D90B3E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38582 Genomic DNA. Translation: BAA07588.1.
U00096 Genomic DNA. Translation: AAC73330.1.
AP009048 Genomic DNA. Translation: BAA77896.1.
PIRiC64747.
RefSeqiNP_414761.1. NC_000913.3.
WP_000729703.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73330; AAC73330; b0226.
BAA77896; BAA77896; BAA77896.
GeneIDi944914.
KEGGiecj:JW0216.
eco:b0226.
PATRICi32115567. VBIEscCol129921_0228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38582 Genomic DNA. Translation: BAA07588.1.
U00096 Genomic DNA. Translation: AAC73330.1.
AP009048 Genomic DNA. Translation: BAA77896.1.
PIRiC64747.
RefSeqiNP_414761.1. NC_000913.3.
WP_000729703.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q2UX-ray1.80A/C/E/G/I/K/M/O1-86[»]
ProteinModelPortaliQ47150.
SMRiQ47150. Positions 3-86.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259772. 55 interactions.
DIPiDIP-9446N.
IntActiQ47150. 2 interactions.
STRINGi511145.b0226.

Proteomic databases

PaxDbiQ47150.
PRIDEiQ47150.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73330; AAC73330; b0226.
BAA77896; BAA77896; BAA77896.
GeneIDi944914.
KEGGiecj:JW0216.
eco:b0226.
PATRICi32115567. VBIEscCol129921_0228.

Organism-specific databases

EchoBASEiEB2936.
EcoGeneiEG13142. dinJ.

Phylogenomic databases

eggNOGiENOG4105QHH. Bacteria.
COG3077. LUCA.
HOGENOMiHOG000008424.
KOiK07473.
OMAiFEVRIPN.
OrthoDBiEOG6SJJS7.

Enzyme and pathway databases

BioCyciEcoCyc:G6110-MONOMER.
ECOL316407:JW0216-MONOMER.
MetaCyc:G6110-MONOMER.

Miscellaneous databases

PROiQ47150.

Gene expression databases

CollecTFiEXPREG_00000df0.

Family and domain databases

InterProiIPR026262. DinJ.
IPR007337. RelB/DinJ.
[Graphical view]
PfamiPF04221. RelB. 1 hit.
[Graphical view]
PIRSFiPIRSF003108. DinJ. 1 hit.
TIGRFAMsiTIGR02384. RelB_DinJ. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "dinP, a new gene in Escherichia coli, whose product shows similarities to UmuC and its homologues."
    Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.
    Mutat. Res. 347:1-7(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Escherichia coli dinJ-yafQ genes act as a toxin-antitoxin module."
    Motiejunaite R., Armalyte J., Markuckas A., Suziedeliene E.
    FEMS Microbiol. Lett. 268:112-119(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTITOXIN, SUBUNIT.
    Strain: K12 / BW25113.
  6. "Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage."
    Prysak M.H., Mozdzierz C.J., Cook A.M., Zhu L., Zhang Y., Inouye M., Woychik N.A.
    Mol. Microbiol. 71:1071-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTITOXIN, CLEAVAGE BY LON AND CLPX PROTEASES, SUBUNIT, DNA-BINDING, INDUCTION.
    Strain: K12 / BW25113 and K12 / DH5-alpha.
  7. "A differential effect of E. coli toxin-antitoxin systems on cell death in liquid media and biofilm formation."
    Kolodkin-Gal I., Verdiger R., Shlosberg-Fedida A., Engelberg-Kulka H.
    PLoS ONE 4:E6785-E6785(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BIOFILM FORMATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Entry informationi

Entry nameiDINJ_ECOLI
AccessioniPrimary (citable) accession number: Q47150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 13, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.