ID   GHOT_ECOL6              Reviewed;          57 AA.
AC   P64647; P58038;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Toxin GhoT {ECO:0000305};
GN   Name=ghoT {ECO:0000305}; OrderedLocusNames=c5136;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Toxic component of a type V toxin-antitoxin (TA) system.
CC       Causes membrane damage when induced by MqsR, slowing cell growth and
CC       leading to the formation of dormant persister cells; involved with
CC       GhoS, its antitoxin, in reducing cell growth during antibacterial
CC       stress. Its toxic effects are neutralized by GhoS, which digests ghoT
CC       transcripts in a sequence-specific manner.
CC       {ECO:0000250|UniProtKB:P64646}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P64646}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GhoT/OrtT toxin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN83558.1; -; Genomic_DNA.
DR   RefSeq; WP_001173343.1; NC_004431.1.
DR   AlphaFoldDB; P64647; -.
DR   STRING; 199310.c5136; -.
DR   EnsemblBacteria; AAN83558; AAN83558; c5136.
DR   GeneID; 66671960; -.
DR   KEGG; ecc:c5136; -.
DR   HOGENOM; CLU_189012_0_0_6; -.
DR   OMA; ITWYLAR; -.
DR   BioCyc; ECOL199310:C5136-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019689; Toxin_GhoT/OrtT.
DR   Pfam; PF10753; Toxin_GhoT_OrtT; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Toxin-antitoxin system;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..57
FT                   /note="Toxin GhoT"
FT                   /id="PRO_0000169737"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   57 AA;  6555 MW;  A3670A19500F75D6 CRC64;
     MALFSKILIF YVIGVNISFV IIWFISHEKT HIRLLSAFLV GITWPMSLPV ALLFSLF