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Toxin GhoT

 GHOT_ECOLI              Reviewed;          57 AA.
P64646; P58038; Q2EEU1; Q2M6H5;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
05-JUL-2017, entry version 87.
RecName: Full=Toxin GhoT {ECO:0000303|PubMed:22941047};
Name=ghoT {ECO:0000303|PubMed:22941047}; Synonyms=yjdO;
OrderedLocusNames=b4559, JW5732;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[3]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / BW25113;
PubMed=22941047; DOI=10.1038/nchembio.1062;
Wang X., Lord D.M., Cheng H.Y., Osbourne D.O., Hong S.H.,
Sanchez-Torres V., Quiroga C., Zheng K., Herrmann T., Peti W.,
Benedik M.J., Page R., Wood T.K.;
"A new type V toxin-antitoxin system where mRNA for toxin GhoT is
cleaved by antitoxin GhoS.";
Nat. Chem. Biol. 8:855-861(2012).
[4]
INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / BW25113;
PubMed=23289863; DOI=10.1111/1462-2920.12063;
Wang X., Lord D.M., Hong S.H., Peti W., Benedik M.J., Page R.,
Wood T.K.;
"Type II toxin/antitoxin MqsR/MqsA controls type V toxin/antitoxin
GhoT/GhoS.";
Environ. Microbiol. 15:1734-1744(2013).
[5]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
OF MET-1; ILE-21 AND PHE-38.
PubMed=24373067; DOI=10.1111/1462-2920.12373;
Cheng H.Y., Soo V.W., Islam S., McAnulty M.J., Benedik M.J.,
Wood T.K.;
"Toxin GhoT of the GhoT/GhoS toxin/antitoxin system damages the cell
membrane to reduce adenosine triphosphate and to reduce growth under
stress.";
Environ. Microbiol. 16:1741-1754(2014).
-!- FUNCTION: Toxic component of a type V toxin-antitoxin (TA) module.
Causes membrane damage when induced by MqsR, slowing cell growth
and increasing the formation of dormant persister cells; involved
with GhoS, its antitoxin, in reducing cell growth during
antibacterial stress (PubMed:24373067). Overexpression causes cell
lysis, forming ghost cells; both effects are neutralized by
expression of GhoS. Overexpression in the presence of ampicillin
increases persister cell formation (persister cells exhibit
antibiotic tolerance without genetic change) (PubMed:22941047).
Overexpression causes about 90-fold reduction in cellular ATP
levels and dissipates the membrane potential (PubMed:24373067).
{ECO:0000269|PubMed:22941047, ECO:0000269|PubMed:24373067}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000305|PubMed:24373067}; Multi-pass membrane protein
{ECO:0000305}. Note=Localizes to the cell pole.
{ECO:0000269|PubMed:24373067}.
-!- INDUCTION: Expression controlled by its antitoxin GhoS, which
digests ghoT transcripts in a sequence-specific manner
(PubMed:22941047). Post-transcriptionally regulated by MqsR which
acts on the ghoST transcript selectively, degrading the ghoS
segment while leaving ghoT intact; conditions which induce MqsR
(e.g. overexpression, nalidixic acid, azolocillin or H(2)O(2))
decrease ghoS expression and thus increase ghoT transcripts
(PubMed:23289863). {ECO:0000269|PubMed:22941047,
ECO:0000269|PubMed:23289863}.
-!- DISRUPTION PHENOTYPE: No visible effect in the absence of stress
(PubMed:24373067). Reduces MqsR-mediated persistence
(overexpression of MqsR increases persister cell formation).
Decreased biofilm formation after 8 hours at 30 and 37 degrees
Celsius, biofilm production has risen by 24 hours. Slight decrease
in swimming motility (PubMed:22941047). Cells grown in 20 ug/ml
ampicillin in the absence of ghoT and which overexpress MqsR
elongate, suggesting MqsR inhibits cell elongation via ghoT
(PubMed:23289863). When single mutant is grown in the presence of
antibiotics carbenicillin or cefoxitin initial metabolism is
significantly increased over that of wild-type, after 14 hours
wild-type is slighlty less active. In a double ghoS-ghoT mutant in
presence of the 2 antibiotics metabolism is significantly
increased over that of wild-type, but by 9 hours wild-type has
caught up and eventually has slightly greater metablic rates
(PubMed:24373067). {ECO:0000269|PubMed:22941047,
ECO:0000269|PubMed:23289863, ECO:0000269|PubMed:24373067}.
-!- SIMILARITY: Belongs to the GhoT/OrtT toxin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U00096; ABD18711.1; -; Genomic_DNA.
EMBL; AP009048; BAE78131.1; -; Genomic_DNA.
RefSeq; WP_001173343.1; NZ_LN832404.1.
RefSeq; YP_588474.1; NC_000913.3.
ProteinModelPortal; P64646; -.
BioGrid; 4261768; 10.
STRING; 316385.ECDH10B_4321; -.
PaxDb; P64646; -.
PRIDE; P64646; -.
EnsemblBacteria; ABD18711; ABD18711; b4559.
EnsemblBacteria; BAE78131; BAE78131; BAE78131.
GeneID; 1450308; -.
KEGG; ecj:JW5732; -.
KEGG; eco:b4559; -.
PATRIC; fig|511145.12.peg.4260; -.
EcoGene; EG14342; ghoT.
HOGENOM; HOG000219287; -.
KO; K18839; -.
BioCyc; EcoCyc:MONOMER0-2694; -.
PRO; PR:P64646; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0060187; C:cell pole; IDA:EcoCyc.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008219; P:cell death; IMP:EcoCyc.
InterPro; IPR019689; Toxin_GhoT/OrtT.
Pfam; PF10753; Toxin_GhoT_OrtT; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome; Membrane;
Reference proteome; Toxin; Transmembrane; Transmembrane helix.
CHAIN 1 57 Toxin GhoT.
/FTId=PRO_0000169735.
TRANSMEM 7 27 Helical. {ECO:0000255}.
TRANSMEM 37 57 Helical. {ECO:0000255}.
MUTAGEN 1 1 M->T: Not toxic in a disrupted ghoS
strain as no protein produced.
{ECO:0000269|PubMed:24373067}.
MUTAGEN 21 21 I->R: Protein remains toxic.
{ECO:0000269|PubMed:24373067}.
MUTAGEN 38 38 F->R: Not toxic, protein still targeted
to cell pole. No change in intracellular
ATP levels, no dissipation of the
membrane potential.
{ECO:0000269|PubMed:24373067}.
SEQUENCE 57 AA; 6555 MW; A3670A19500F75D6 CRC64;
MALFSKILIF YVIGVNISFV IIWFISHEKT HIRLLSAFLV GITWPMSLPV ALLFSLF


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