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Protein

Toxin GhoT

Gene

ghoT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

GO - Biological processi

  • cell death Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Toxin

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-2694.
ECOL316407:JW5732-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Toxin GhoT1 Publication
Gene namesi
Name:ghoT1 Publication
Synonyms:yjdO
Ordered Locus Names:b4559, JW5732
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14342. ghoT.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2721HelicalSequence analysisAdd
BLAST
Transmembranei37 – 5721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell pole Source: EcoCyc
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: EcoCyc
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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 µg/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).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → T: Not toxic in a disrupted ghoS strain as no protein produced. 1 Publication
Mutagenesisi21 – 211I → R: Protein remains toxic. 1 Publication
Mutagenesisi38 – 381F → R: Not toxic, protein still targeted to cell pole. No change in intracellular ATP levels, no dissipation of the membrane potential. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5757Toxin GhoTPRO_0000169735Add
BLAST

Proteomic databases

PaxDbiP64646.

Expressioni

Inductioni

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 H2O2) decrease ghoS expression and thus increase ghoT transcripts (PubMed:23289863).2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4261768. 10 interactions.
STRINGi511145.b4559.

Structurei

3D structure databases

ProteinModelPortaliP64646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GhoT/OrtT toxin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000219287.
KOiK18839.
OrthoDBiEOG6DG2Z7.

Family and domain databases

InterProiIPR019689. Toxin_GhoT/OrtT.
[Graphical view]
PfamiPF10753. DUF2566. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P64646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALFSKILIF YVIGVNISFV IIWFISHEKT HIRLLSAFLV GITWPMSLPV

ALLFSLF
Length:57
Mass (Da):6,555
Last modified:October 11, 2004 - v1
Checksum:iA3670A19500F75D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: ABD18711.1.
AP009048 Genomic DNA. Translation: BAE78131.1.
RefSeqiWP_001173343.1. NZ_LN832404.1.
YP_588474.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiABD18711; ABD18711; b4559.
BAE78131; BAE78131; BAE78131.
GeneIDi1450308.
KEGGiecj:JW5732.
eco:b4559.
PATRICi32123823. VBIEscCol129921_4260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: ABD18711.1.
AP009048 Genomic DNA. Translation: BAE78131.1.
RefSeqiWP_001173343.1. NZ_LN832404.1.
YP_588474.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP64646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261768. 10 interactions.
STRINGi511145.b4559.

Proteomic databases

PaxDbiP64646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD18711; ABD18711; b4559.
BAE78131; BAE78131; BAE78131.
GeneIDi1450308.
KEGGiecj:JW5732.
eco:b4559.
PATRICi32123823. VBIEscCol129921_4260.

Organism-specific databases

EcoGeneiEG14342. ghoT.

Phylogenomic databases

HOGENOMiHOG000219287.
KOiK18839.
OrthoDBiEOG6DG2Z7.

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-2694.
ECOL316407:JW5732-MONOMER.

Miscellaneous databases

PROiP64646.

Family and domain databases

InterProiIPR019689. Toxin_GhoT/OrtT.
[Graphical view]
PfamiPF10753. DUF2566. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS."
    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.
    Nat. Chem. Biol. 8:855-861(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / BW25113.
  4. "Type II toxin/antitoxin MqsR/MqsA controls type V toxin/antitoxin GhoT/GhoS."
    Wang X., Lord D.M., Hong S.H., Peti W., Benedik M.J., Page R., Wood T.K.
    Environ. Microbiol. 15:1734-1744(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / BW25113.
  5. "Toxin GhoT of the GhoT/GhoS toxin/antitoxin system damages the cell membrane to reduce adenosine triphosphate and to reduce growth under stress."
    Cheng H.Y., Soo V.W., Islam S., McAnulty M.J., Benedik M.J., Wood T.K.
    Environ. Microbiol. 16:1741-1754(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF MET-1; ILE-21 AND PHE-38.

Entry informationi

Entry nameiGHOT_ECOLI
AccessioniPrimary (citable) accession number: P64646
Secondary accession number(s): P58038, Q2EEU1, Q2M6H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 20, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.