TISB_ECOLI
ID TISB_ECOLI Reviewed; 29 AA.
AC A5A627;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Small toxic protein TisB;
DE AltName: Full=LexA-regulated protein TisB;
GN Name=tisB; Synonyms=ysdB; OrderedLocusNames=b4618, JW3649;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP REGULATION BY LEXA, AND INDUCTION.
RC STRAIN=K12 / RW118;
RX PubMed=10760155; DOI=10.1046/j.1365-2958.2000.01826.x;
RA Fernandez De Henestrosa A.R., Ogi T., Aoyagi S., Chafin D., Hayes J.J.,
RA Ohmori H., Woodgate R.;
RT "Identification of additional genes belonging to the LexA regulon in
RT Escherichia coli.";
RL Mol. Microbiol. 35:1560-1572(2000).
RN [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=15620655; DOI=10.1016/j.cub.2004.12.003;
RA Vogel J., Argaman L., Wagner E.G.H., Altuvia S.;
RT "The small RNA IstR inhibits synthesis of an SOS-induced toxic peptide.";
RL Curr. Biol. 14:2271-2276(2004).
RN [5]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=17499044; DOI=10.1016/j.molcel.2007.04.003;
RA Darfeuille F., Unoson C., Vogel J., Wagner E.G.H.;
RT "An antisense RNA inhibits translation by competing with standby
RT ribosomes.";
RL Mol. Cell 26:381-392(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18761622; DOI=10.1111/j.1365-2958.2008.06416.x;
RA Unoson C., Wagner E.G.H.;
RT "A small SOS-induced toxin is targeted against the inner membrane in
RT Escherichia coli.";
RL Mol. Microbiol. 70:258-270(2008).
RN [7]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18710431; DOI=10.1111/j.1365-2958.2008.06394.x;
RA Fozo E.M., Kawano M., Fontaine F., Kaya Y., Mendieta K.S., Jones K.L.,
RA Ocampo A., Rudd K.E., Storz G.;
RT "Repression of small toxic protein synthesis by the Sib and OhsC small
RT RNAs.";
RL Mol. Microbiol. 70:1076-1093(2008).
RN [8]
RP FUNCTION AS A TOXIN, AND SUBCELLULAR LOCATION.
RX PubMed=24513967; DOI=10.1159/000357949;
RA Yamaguchi Y., Tokunaga N., Inouye M., Phadtare S.;
RT "Characterization of LdrA (long direct repeat A) protein of Escherichia
RT coli.";
RL J. Mol. Microbiol. Biotechnol. 24:91-97(2014).
CC -!- FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system
CC (PubMed:18761622) (Probable). Overexpression causes cessation of
CC growth, induces stress-response, a number of membrane protein genes,
CC and leads to cell death (PubMed:15620655, PubMed:18761622,
CC PubMed:18710431). Inhibits ATP synthesis, ATP levels drop drastically
CC quickly after induction (PubMed:18761622, PubMed:24513967). Part of the
CC programmed response to DNA damage; damage leads to increased
CC accumulation of the protein which slows or stops bacterial growth,
CC probably allowing DNA repair before cells continue to grow
CC (PubMed:15620655, PubMed:18761622). {ECO:0000269|PubMed:15620655,
CC ECO:0000269|PubMed:18710431, ECO:0000269|PubMed:18761622,
CC ECO:0000269|PubMed:24513967, ECO:0000305|PubMed:18710431}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:18761622,
CC ECO:0000269|PubMed:24513967}; Single-pass membrane protein
CC {ECO:0000269|PubMed:18761622, ECO:0000269|PubMed:24513967}.
CC -!- INDUCTION: Part of the SOS-response regulon, controlled by LexA;
CC repressed by LexA, induced by DNA damage (PubMed:10760155). Antisense
CC sRNA IstR-1 inhibits toxicity by inhibiting translation of tisAB mRNA;
CC subsequent RNase 3 cleavage leads to a truncated mRNA. IstR-1
CC sequesters a standby ribosome binding site in the tisAB mRNA; as the
CC levels of IstR-1 decrease during the SOS response this site opens and
CC ribosomes are able to bind to initiate translation further downstream
CC (PubMed:15620655, PubMed:17499044). {ECO:0000269|PubMed:10760155,
CC ECO:0000269|PubMed:15620655, ECO:0000269|PubMed:17499044}.
CC -!- DISRUPTION PHENOTYPE: Competition experiments between isogenic strains
CC with or without the tisB/istR-1 region were performed. In the presence
CC of DNA-damaging agents deletion strains were disadvantaged and were
CC almost extinct by 4 days. {ECO:0000269|PubMed:18761622}.
CC -!- CAUTION: Originally tisA and tisB were fused into one ORF by frameshift
CC reconstruction. TisA is probably a pseudogene. {ECO:0000305}.
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DR EMBL; U00096; ABP93456.1; -; Genomic_DNA.
DR EMBL; AP009048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_001054909.1; NZ_SSZK01000035.1.
DR RefSeq; YP_001165331.1; NC_000913.3.
DR AlphaFoldDB; A5A627; -.
DR STRING; 511145.b4618; -.
DR TCDB; 1.C.103.1.1; the pore-forming toxin, tisb (tisb) family.
DR PaxDb; A5A627; -.
DR PRIDE; A5A627; -.
DR EnsemblBacteria; ABP93456; ABP93456; b4618.
DR GeneID; 5061527; -.
DR KEGG; eco:b4618; -.
DR PATRIC; fig|83333.103.peg.4606; -.
DR BioCyc; EcoCyc:MON0-1922; -.
DR PRO; PR:A5A627; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005253; F:anion channel activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0022611; P:dormancy process; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEP:EcoCyc.
DR InterPro; IPR025211; TisB_toxin.
DR Pfam; PF13939; TisB_toxin; 1.
DR TIGRFAMs; TIGR04459; TisB_tox; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Toxin-antitoxin system; Transmembrane; Transmembrane helix.
FT CHAIN 1..29
FT /note="Small toxic protein TisB"
FT /id="PRO_0000311834"
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 29 AA; 3222 MW; 6F3B7FE3D9FEFC80 CRC64;
MNLVDIAILI LKLIVAALQL LDAVLKYLK
