RELB_ECOLI
ID RELB_ECOLI Reviewed; 79 AA.
AC P0C079; P07007;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Antitoxin RelB {ECO:0000303|PubMed:9767574};
GN Name=relB; OrderedLocusNames=b1564, JW1556;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON, AND MUTAGENESIS OF ALA-39 AND
RP PRO-45.
RC STRAIN=K12 / CS520;
RX PubMed=2990907; DOI=10.1002/j.1460-2075.1985.tb03739.x;
RA Bech F.W., Joergensen S.T., Diderichsen B., Karlstroem O.H.;
RT "Sequence of the relB transcription unit from Escherichia coli and
RT identification of the relB gene.";
RL EMBO J. 4:1059-1066(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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, FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, AND
RP INDUCTION.
RX PubMed=9767574; DOI=10.1046/j.1365-2958.1998.00993.x;
RA Gotfredsen M., Gerdes K.;
RT "The Escherichia coli relBE genes belong to a new toxin-antitoxin gene
RT family.";
RL Mol. Microbiol. 29:1065-1076(1998).
RN [6]
RP FUNCTION, SUBUNIT, AND DNA-BINDING.
RX PubMed=11274135; DOI=10.1128/jb.183.8.2700-2703.2001;
RA Galvani C., Terry J., Ishiguro E.E.;
RT "Purification of the RelB and RelE proteins of Escherichia coli: RelE binds
RT to RelB and to ribosomes.";
RL J. Bacteriol. 183:2700-2703(2001).
RN [7]
RP FUNCTION, CLEAVAGE BY LON PROTEASE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11717402; DOI=10.1073/pnas.251327898;
RA Christensen S.K., Mikkelsen M., Pedersen K., Gerdes K.;
RT "RelE, a global inhibitor of translation, is activated during nutritional
RT stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14328-14333(2001).
RN [8]
RP FUNCTION AS AN ANTITOXIN.
RC STRAIN=K12;
RX PubMed=12123459; DOI=10.1046/j.1365-2958.2002.03027.x;
RA Pedersen K., Christensen S.K., Gerdes K.;
RT "Rapid induction and reversal of a bacteriostatic condition by controlled
RT expression of toxins and antitoxins.";
RL Mol. Microbiol. 45:501-510(2002).
RN [9]
RP FUNCTION, INDUCTION, DOMAIN, AND DNA-BINDING.
RC STRAIN=K12;
RX PubMed=18532983; DOI=10.1111/j.1365-2958.2008.06313.x;
RA Overgaard M., Borch J., Joergensen M.G., Gerdes K.;
RT "Messenger RNA interferase RelE controls relBE transcription by conditional
RT cooperativity.";
RL Mol. Microbiol. 69:841-857(2008).
RN [10]
RP FUNCTION, SUBUNIT, INDUCTION, CLEAVAGE BY LON PROTEASE, DNA-BINDING, AND
RP MUTAGENESIS OF ARG-7; ILE-8; LYS-13 AND SER-28.
RC STRAIN=K12;
RX PubMed=19747491; DOI=10.1016/j.jmb.2009.09.006;
RA Overgaard M., Borch J., Gerdes K.;
RT "RelB and RelE of Escherichia coli form a tight complex that represses
RT transcription via the ribbon-helix-helix motif in RelB.";
RL J. Mol. Biol. 394:183-196(2009).
RN [11]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [12]
RP FUNCTION IN CELL DEATH, AND DISRUPTION 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 [13]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22210768; DOI=10.1128/jb.06628-11;
RA Tashiro Y., Kawata K., Taniuchi A., Kakinuma K., May T., Okabe S.;
RT "RelE-mediated dormancy is enhanced at high cell density in Escherichia
RT coli.";
RL J. Bacteriol. 194:1169-1176(2012).
RN [14]
RP INDUCTION BY OTHER TA SYSTEMS.
RC STRAIN=K12 / BW25113;
RX PubMed=23432955; DOI=10.1186/1471-2180-13-45;
RA Kasari V., Mets T., Tenson T., Kaldalu N.;
RT "Transcriptional cross-activation between toxin-antitoxin systems of
RT Escherichia coli.";
RL BMC Microbiol. 13:45-45(2013).
RN [15]
RP STRUCTURE BY NMR OF 1-50, FUNCTION, DNA-BINDING, SUBUNIT, INDUCTION,
RP DOMAINS, AND MUTAGENESIS OF ARG-7; 66-LEU--LEU-79 AND 71-PRO--LEU-79.
RX PubMed=18501926; DOI=10.1016/j.jmb.2008.04.039;
RA Li G.Y., Zhang Y., Inouye M., Ikura M.;
RT "Structural mechanism of transcriptional autorepression of the Escherichia
RT coli RelB/RelE antitoxin/toxin module.";
RL J. Mol. Biol. 380:107-119(2008).
RN [16]
RP STRUCTURE BY NMR OF 47-79 IN COMPLEX WITH RELE, AND SUBUNIT.
RX PubMed=19297318; DOI=10.1074/jbc.m809656200;
RA Li G.Y., Zhang Y., Inouye M., Ikura M.;
RT "Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module
RT involves a helix displacement near an mRNA interferase active site.";
RL J. Biol. Chem. 284:14628-14636(2009).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH RELB, FUNCTION,
RP SUBUNIT, AND INDUCTION.
RX PubMed=22981948; DOI=10.1016/j.str.2012.08.017;
RA Boggild A., Sofos N., Andersen K.R., Feddersen A., Easter A.D.,
RA Passmore L.A., Brodersen D.E.;
RT "The crystal structure of the intact E. coli RelBE toxin-antitoxin complex
RT provides the structural basis for conditional cooperativity.";
RL Structure 20:1641-1648(2012).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Counteracts the effect of cognate toxin RelE via direct protein-protein
CC interaction, preventing RelE from entering the ribosome A site and thus
CC inhibiting its endoribonuclease activity. An autorepressor of relBE
CC operon transcription. 2 RelB dimers bind to 2 operator sequences; DNA-
CC binding and repression is stronger when complexed with
CC toxin/corepressor RelE by conditional cooperativity (PubMed:18501926,
CC PubMed:22981948). Increased transcription rate of relBE and activation
CC of relE is consistent with a lower level of RelB in starved cells due
CC to degradation of RelB by protease Lon. {ECO:0000269|PubMed:11274135,
CC ECO:0000269|PubMed:11717402, ECO:0000269|PubMed:12123459,
CC ECO:0000269|PubMed:18501926, ECO:0000269|PubMed:18532983,
CC ECO:0000269|PubMed:19707553, ECO:0000269|PubMed:19747491,
CC ECO:0000269|PubMed:22210768, ECO:0000269|PubMed:22981948,
CC ECO:0000269|PubMed:9767574}.
CC -!- FUNCTION: Seems to be a principal mediator of cell death in liquid
CC media. {ECO:0000269|PubMed:19707553}.
CC -!- SUBUNIT: Homotetramer formed by dimerization of dimers in solution
CC (PubMed:19747491, PubMed:18501926). Forms an RelB(2)-RelE(2)
CC heterotetramer (PubMed:18501926, PubMed:22981948). Also forms an
CC RelB(2)-RelE heterotrimer (PubMed:18532983, PubMed:19747491). The
CC RelB(2)-RelE complex is probably the one that binds DNA and represses
CC transcription, possibly as 2 heterotrimers, 1 bound to each of 2
CC operators (PubMed:22981948, PubMed:19747491).
CC {ECO:0000269|PubMed:11274135, ECO:0000269|PubMed:18501926,
CC ECO:0000269|PubMed:18532983, ECO:0000269|PubMed:19297318,
CC ECO:0000269|PubMed:19747491, ECO:0000269|PubMed:22981948}.
CC -!- INTERACTION:
CC P0C079; P0C077: relE; NbExp=3; IntAct=EBI-1124503, EBI-549378;
CC -!- INDUCTION: By amino acid starvation, by glucose starvation and by
CC chloramphenicol; induction is independent of ppGpp. Autorepressed by
CC RelB, RelE acts as a corepressor (PubMed:9767574, PubMed:19747491,
CC PubMed:18501926, PubMed:22981948). Member of the relBEF operon
CC (PubMed:2990907). Operon induced by ectopic expression of toxins HicA,
CC HipA, MazF, MqsR and RelE, but not by YafQ (PubMed:23432955).
CC {ECO:0000269|PubMed:11717402, ECO:0000269|PubMed:18501926,
CC ECO:0000269|PubMed:18532983, ECO:0000269|PubMed:19747491,
CC ECO:0000269|PubMed:22981948, ECO:0000269|PubMed:23432955,
CC ECO:0000269|PubMed:2990907, ECO:0000269|PubMed:9767574}.
CC -!- DOMAIN: Dimerizes and binds DNA via its N-terminus (residues 1-50),
CC binds toxin RelE via the C-terminus (residues 47-79) (PubMed:18501926,
CC PubMed:18532983). Tetramerization probably requires amino acids between
CC residues 66 and 71 (PubMed:18501926). {ECO:0000269|PubMed:18501926,
CC ECO:0000269|PubMed:18532983}.
CC -!- PTM: Probably degraded by Lon protease during amino acid starvation
CC (PubMed:11717402). Degraded in vitro by Lon (PubMed:19747491).
CC {ECO:0000269|PubMed:11717402, ECO:0000269|PubMed:19747491}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted if a copy of relE
CC remains in the cell. Cells missing relBE have a higher steady-state
CC level of translation during amino acid starvation than wild-type cells.
CC They survive antibiotic treatment in log phase better than wild-type
CC cells. Cells missing mazE-mazF survive hydroxyurea treatment better
CC than wild-type; further disruption of relE-relB and tonB yields even
CC better survival (PubMed:20005847). {ECO:0000269|PubMed:11717402,
CC ECO:0000269|PubMed:19707553, ECO:0000269|PubMed:20005847}.
CC -!- MISCELLANEOUS: A number of site directed mutants give rise to a delayed
CC relaxed phenotype; RNA synthesis resumes 10 minutes after amino acid
CC starvation, an unusually slow recovery from periods of starvation,
CC accumulation of a translation inhibitor. {ECO:0000303|PubMed:2990907}.
CC -!- MISCELLANEOUS: There are estimated to be 550-1100 RelB and 50-100 RelE
CC molecules in rapidly growing cells of MG1655; as they have quite high
CC affinity for each other (dissociation constant of 0.33 nM) there is
CC probably less than 1 free RelE molecule per cell. The RelB(2)-RelE
CC complex has a half-life of over 70 minutes.
CC {ECO:0000269|PubMed:19747491}.
CC -!- SIMILARITY: Belongs to the RelB/DinJ antitoxin family. {ECO:0000305}.
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DR EMBL; X02405; CAA26250.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74637.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15263.1; -; Genomic_DNA.
DR PIR; A22830; BVECRB.
DR RefSeq; NP_416082.1; NC_000913.3.
DR RefSeq; WP_000534858.1; NZ_SSUV01000001.1.
DR PDB; 2K29; NMR; -; A/B=1-50.
DR PDB; 2KC8; NMR; -; B=47-79.
DR PDB; 4FXE; X-ray; 2.75 A; A/B/C=1-79.
DR PDBsum; 2K29; -.
DR PDBsum; 2KC8; -.
DR PDBsum; 4FXE; -.
DR AlphaFoldDB; P0C079; -.
DR BMRB; P0C079; -.
DR SMR; P0C079; -.
DR BioGRID; 4260244; 61.
DR ComplexPortal; CPX-1081; RelBE toxin-antitoxin complex.
DR DIP; DIP-48258N; -.
DR IntAct; P0C079; 6.
DR STRING; 511145.b1564; -.
DR jPOST; P0C079; -.
DR PaxDb; P0C079; -.
DR PRIDE; P0C079; -.
DR EnsemblBacteria; AAC74637; AAC74637; b1564.
DR EnsemblBacteria; BAA15263; BAA15263; BAA15263.
DR GeneID; 39497046; -.
DR GeneID; 67515104; -.
DR GeneID; 948308; -.
DR KEGG; ecj:JW1556; -.
DR KEGG; eco:b1564; -.
DR PATRIC; fig|1411691.4.peg.698; -.
DR EchoBASE; EB0829; -.
DR eggNOG; COG3077; Bacteria.
DR HOGENOM; CLU_169573_0_0_6; -.
DR OMA; TINIRVN; -.
DR PhylomeDB; P0C079; -.
DR BioCyc; EcoCyc:EG10836-MON; -.
DR BioCyc; MetaCyc:EG10836-MON; -.
DR EvolutionaryTrace; P0C079; -.
DR PRO; PR:P0C079; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_000008a0; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0110001; C:toxin-antitoxin complex; IPI:ComplexPortal.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0044010; P:single-species biofilm formation; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; EXP:EcoCyc.
DR DisProt; DP02950; -.
DR Gene3D; 1.10.1220.10; -; 1.
DR InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR InterPro; IPR007337; RelB/DinJ.
DR PANTHER; PTHR38781; PTHR38781; 1.
DR Pfam; PF04221; RelB; 1.
DR TIGRFAMs; TIGR02384; RelB_DinJ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Stress response;
KW Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..79
FT /note="Antitoxin RelB"
FT /id="PRO_0000097243"
FT MUTAGEN 7
FT /note="R->A: Loss of DNA binding, 100-fold derepression of
FT operon, still binds RelE."
FT /evidence="ECO:0000269|PubMed:18501926,
FT ECO:0000269|PubMed:19747491"
FT MUTAGEN 8
FT /note="I->A: 43-fold derepression of operon, partial loss
FT of DNA-binding, still binds RelE."
FT /evidence="ECO:0000269|PubMed:19747491"
FT MUTAGEN 13
FT /note="K->A: 83-fold derepression of operon, loss of DNA-
FT binding, still binds RelE."
FT /evidence="ECO:0000269|PubMed:19747491"
FT MUTAGEN 28
FT /note="S->L,R: 100-fold derepression of operon, loss of
FT DNA-binding, still binds RelE."
FT /evidence="ECO:0000269|PubMed:19747491"
FT MUTAGEN 39
FT /note="A->T: In relB101; a delayed relaxed phenotype."
FT /evidence="ECO:0000269|PubMed:2990907"
FT MUTAGEN 45
FT /note="P->L: In relB102; a delayed relaxed phenotype."
FT /evidence="ECO:0000269|PubMed:2990907"
FT MUTAGEN 45
FT /note="P->T: In relB35; a delayed relaxed phenotype."
FT /evidence="ECO:0000269|PubMed:2990907"
FT MUTAGEN 66..79
FT /note="Missing: Protein no longer tetramerizes."
FT /evidence="ECO:0000269|PubMed:18501926"
FT MUTAGEN 71..79
FT /note="Missing: Protein still tetramerizes."
FT /evidence="ECO:0000269|PubMed:18501926"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4FXE"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:4FXE"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:4FXE"
FT HELIX 49..67
FT /evidence="ECO:0007829|PDB:4FXE"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4FXE"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4FXE"
SQ SEQUENCE 79 AA; 9071 MW; 3DD2107337226FAD CRC64;
MGSINLRIDD ELKARSYAAL EKMGVTPSEA LRLMLEYIAD NERLPFKQTL LSDEDAELVE
IVKERLRNPK PVRVTLDEL
