DINJ_ECOBD
ID DINJ_ECOBD Reviewed; 86 AA.
AC A0A140ND86;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Antitoxin DinJ;
GN Name=dinJ; OrderedLocusNames=ECBD_3396;
OS Escherichia coli (strain B / BL21-DE3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=469008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT "Complete sequence of Escherichia coli BL21(DE3).";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4ML0}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH YAFQ, FUNCTION,
RP SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF ARG-8; LYS-16; 31-SER--ARG-35;
RP PHE-49 AND 59-ILE--ILE-62.
RC STRAIN=B / BL21-DE3;
RX PubMed=24923448; DOI=10.1074/jbc.m114.559773;
RA Liang Y., Gao Z., Wang F., Zhang Y., Dong Y., Liu Q.;
RT "Structural and functional characterization of Escherichia coli toxin-
RT antitoxin complex DinJ-YafQ.";
RL J. Biol. Chem. 289:21191-21202(2014).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system
CC (PubMed:24923448). A labile antitoxin that counteracts the effect of
CC cognate toxin YafQ (PubMed:24923448). The YafQ-DinJ heterotetramer
CC binds the consensus sequence 5'-TTTGAGCTACA-3' in the dinJ promoter;
CC DinJ also binds DNA but not as well as the YafQ-DinJ complex
CC (PubMed:24923448). Binding to the dinJ represses expression of the
CC promoter (By similarity). {ECO:0000250|UniProtKB:Q47150,
CC ECO:0000269|PubMed:24923448}.
CC -!- SUBUNIT: Probably a dimer in solution, forms a heterotetramer with
CC antitoxin DinJ, with 2 YafQ-DinJ dimers associated via the N-terminus
CC of the DinJ antitoxins (YafQ-(DinJ)2-YafQ) (PubMed:24923448).
CC {ECO:0000269|PubMed:24923448}.
CC -!- SIMILARITY: Belongs to the RelB/DinJ antitoxin family. {ECO:0000305}.
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DR EMBL; CP001665; ACT30396.1; -; Genomic_DNA.
DR RefSeq; WP_000729704.1; NZ_CP053602.1.
DR PDB; 4ML0; X-ray; 2.10 A; A/C/E/G/I/K/M/O=1-86.
DR PDBsum; 4ML0; -.
DR AlphaFoldDB; A0A140ND86; -.
DR SMR; A0A140ND86; -.
DR STRING; 469008.B21_00225; -.
DR GeneID; 66671455; -.
DR KEGG; ebd:ECBD_3396; -.
DR PATRIC; fig|469008.15.peg.225; -.
DR eggNOG; COG3077; Bacteria.
DR HOGENOM; CLU_154558_12_2_6; -.
DR OMA; FEVRIPN; -.
DR Proteomes; UP000002032; Chromosome.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0015643; F:toxic substance binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0044010; P:single-species biofilm formation; IEA:InterPro.
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; Repressor; Toxin-antitoxin system;
KW Transcription; Transcription regulation.
FT CHAIN 1..86
FT /note="Antitoxin DinJ"
FT /id="PRO_0000440936"
FT MUTAGEN 8
FT /note="R->A: Does not bind to dinJ promoter; when
FT associated with A-16."
FT /evidence="ECO:0000269|PubMed:24923448"
FT MUTAGEN 16
FT /note="K->A: Does not bind to dinJ promoter; when
FT associated with A-8."
FT /evidence="ECO:0000269|PubMed:24923448"
FT MUTAGEN 31..35
FT /note="SDLVR->ADLVA: Does not bind to dinJ promoter."
FT /evidence="ECO:0000269|PubMed:24923448"
FT MUTAGEN 49
FT /note="F->A: No effect in vivo, in vitro forms a complex
FT with toxin YafQ which is not able to cleave RNA, i.e. does
FT not release YafQ. YafQ-DinJ complex binds DNA."
FT /evidence="ECO:0000269|PubMed:24923448"
FT MUTAGEN 59..62
FT /note="IQSI->NQSN: No effect in vivo, in vitro forms a
FT complex with toxin YafQ which is still able to cleave RNA,
FT i.e. has lost antitoxin activity. YafQ-DinJ complex binds
FT DNA."
FT /evidence="ECO:0000269|PubMed:24923448"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4ML0"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4ML0"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4ML0"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:4ML0"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:4ML0"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4ML0"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4ML0"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:4ML0"
SQ SEQUENCE 86 AA; 9392 MW; 9B91EA370D90B3E2 CRC64;
MAANAFVRAR IDEDLKNQAA DVLAGMGLTI SDLVRITLTK VAREKALPFD LREPNQLTIQ
SIKNSEAGVD VHKAKDADDL FDKLGI