GHOT_ECOLI
ID GHOT_ECOLI Reviewed; 57 AA.
AC P64646; P58038; Q2EEU1; Q2M6H5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Toxin GhoT {ECO:0000303|PubMed:22941047};
GN Name=ghoT {ECO:0000303|PubMed:22941047}; Synonyms=yjdO;
GN OrderedLocusNames=b4559, JW5732;
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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=22941047; DOI=10.1038/nchembio.1062;
RA Wang X., Lord D.M., Cheng H.Y., Osbourne D.O., Hong S.H.,
RA Sanchez-Torres V., Quiroga C., Zheng K., Herrmann T., Peti W.,
RA Benedik M.J., Page R., Wood T.K.;
RT "A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved
RT by antitoxin GhoS.";
RL Nat. Chem. Biol. 8:855-861(2012).
RN [4]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=23289863; DOI=10.1111/1462-2920.12063;
RA Wang X., Lord D.M., Hong S.H., Peti W., Benedik M.J., Page R., Wood T.K.;
RT "Type II toxin/antitoxin MqsR/MqsA controls type V toxin/antitoxin
RT GhoT/GhoS.";
RL Environ. Microbiol. 15:1734-1744(2013).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP MET-1; ILE-21 AND PHE-38.
RX PubMed=24373067; DOI=10.1111/1462-2920.12373;
RA Cheng H.Y., Soo V.W., Islam S., McAnulty M.J., Benedik M.J., Wood T.K.;
RT "Toxin GhoT of the GhoT/GhoS toxin/antitoxin system damages the cell
RT membrane to reduce adenosine triphosphate and to reduce growth under
RT stress.";
RL Environ. Microbiol. 16:1741-1754(2014).
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 increasing the formation of dormant persister cells; involved with
CC GhoS, its antitoxin, in reducing cell growth during antibacterial
CC stress (PubMed:24373067). Overexpression causes cell lysis, forming
CC ghost cells; both effects are neutralized by expression of GhoS.
CC Overexpression in the presence of ampicillin increases persister cell
CC formation (persister cells exhibit antibiotic tolerance without genetic
CC change) (PubMed:22941047). Overexpression causes about 90-fold
CC reduction in cellular ATP levels and dissipates the membrane potential
CC (PubMed:24373067). {ECO:0000269|PubMed:22941047,
CC ECO:0000269|PubMed:24373067}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:24373067}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Localizes to the cell pole.
CC {ECO:0000269|PubMed:24373067}.
CC -!- INDUCTION: Expression controlled by its antitoxin GhoS, which digests
CC ghoT transcripts in a sequence-specific manner (PubMed:22941047). Post-
CC transcriptionally regulated by MqsR which acts on the ghoST transcript
CC selectively, degrading the ghoS segment while leaving ghoT intact;
CC conditions which induce MqsR (e.g. overexpression, nalidixic acid,
CC azolocillin or H(2)O(2)) decrease ghoS expression and thus increase
CC ghoT transcripts (PubMed:23289863). {ECO:0000269|PubMed:22941047,
CC ECO:0000269|PubMed:23289863}.
CC -!- DISRUPTION PHENOTYPE: No visible effect in the absence of stress
CC (PubMed:24373067). Reduces MqsR-mediated persistence (overexpression of
CC MqsR increases persister cell formation). Decreased biofilm formation
CC after 8 hours at 30 and 37 degrees Celsius, biofilm production has
CC risen by 24 hours. Slight decrease in swimming motility
CC (PubMed:22941047). Cells grown in 20 ug/ml ampicillin in the absence of
CC ghoT and which overexpress MqsR elongate, suggesting MqsR inhibits cell
CC elongation via ghoT (PubMed:23289863). When single mutant is grown in
CC the presence of antibiotics carbenicillin or cefoxitin initial
CC metabolism is significantly increased over that of wild-type, after 14
CC hours wild-type is slightly less active. In a double ghoS-ghoT mutant
CC in presence of the 2 antibiotics metabolism is significantly increased
CC over that of wild-type, but by 9 hours wild-type has caught up and
CC eventually has slightly greater metabolic rates (PubMed:24373067).
CC {ECO:0000269|PubMed:22941047, ECO:0000269|PubMed:23289863,
CC ECO:0000269|PubMed:24373067}.
CC -!- SIMILARITY: Belongs to the GhoT/OrtT toxin family. {ECO:0000305}.
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DR EMBL; U00096; ABD18711.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78131.1; -; Genomic_DNA.
DR RefSeq; WP_001173343.1; NZ_STEB01000014.1.
DR RefSeq; YP_588474.1; NC_000913.3.
DR AlphaFoldDB; P64646; -.
DR BioGRID; 4261768; 10.
DR STRING; 511145.b4559; -.
DR TCDB; 1.C.130.1.2; the membrane potential-dissipating orphan 10 toxin, (ortt) family.
DR PaxDb; P64646; -.
DR EnsemblBacteria; ABD18711; ABD18711; b4559.
DR EnsemblBacteria; BAE78131; BAE78131; BAE78131.
DR GeneID; 1450308; -.
DR GeneID; 66671960; -.
DR KEGG; ecj:JW5732; -.
DR KEGG; eco:b4559; -.
DR PATRIC; fig|511145.12.peg.4260; -.
DR HOGENOM; CLU_189012_0_0_6; -.
DR OMA; ITWYLAR; -.
DR PhylomeDB; P64646; -.
DR BioCyc; EcoCyc:MON0-2694; -.
DR PRO; PR:P64646; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0060187; C:cell pole; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008219; P:cell death; IMP:EcoCyc.
DR InterPro; IPR019689; Toxin_GhoT/OrtT.
DR Pfam; PF10753; Toxin_GhoT_OrtT; 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..57
FT /note="Toxin GhoT"
FT /id="PRO_0000169735"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 1
FT /note="M->T: Not toxic in a disrupted ghoS strain as no
FT protein produced."
FT /evidence="ECO:0000269|PubMed:24373067"
FT MUTAGEN 21
FT /note="I->R: Protein remains toxic."
FT /evidence="ECO:0000269|PubMed:24373067"
FT MUTAGEN 38
FT /note="F->R: Not toxic, protein still targeted to cell
FT pole. No change in intracellular ATP levels, no dissipation
FT of the membrane potential."
FT /evidence="ECO:0000269|PubMed:24373067"
SQ SEQUENCE 57 AA; 6555 MW; A3670A19500F75D6 CRC64;
MALFSKILIF YVIGVNISFV IIWFISHEKT HIRLLSAFLV GITWPMSLPV ALLFSLF
