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Protein

Endoribonuclease antitoxin GhoS

Gene

ghoS

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

Functioni

Antitoxin component of a type V toxin-antitoxin (TA) system. Neutralizes the toxic effects of toxin GhoT by digesting ghoT transcripts in a sequence-specific manner (PubMed:22941047). In concert with GhoT is involved in reducing cell growth during antibacterial stress (PubMed:24373067). Overexpression leads to transcript level reduction of 20 other mRNAs involved in purine or pyrimidine synthesis and transport. Not seen to bind its own promoter DNA (PubMed:22941047).2 Publications

Miscellaneous

Has a similar 3D-structure to Cas2 proteins.1 Publication
Can be modified to become a classic type II TA toxin (called ArT) which causes cells to become ghost-like, probably by broadening substrate RNA recognition; the toxic activity is independent of ghoT and mqsRA. Antitoxins to this evolved ArT toxin have been artifically evolved from antitoxins mqsA (a type II TA system) and toxI (a type I TA system).1 Publication

GO - Molecular functioni

  • endoribonuclease activity Source: EcoCyc

GO - Biological processi

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processToxin-antitoxin system, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciEcoCyc:G7830-MONOMER
MetaCyc:G7830-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Endoribonuclease antitoxin GhoS1 Publication (EC:3.1.-.-)
Alternative name(s):
Antitoxin GhoS
Gene namesi
Name:ghoS1 Publication
Synonyms:arT1 Publication, yjdK
Ordered Locus Names:b4128, JW4089
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12468 ghoS

Pathology & Biotechi

Disruption phenotypei

Essential; cannot be disrupted unless ghoT is also disrupted; in the double ghoS-ghoT mutant has no visible phenotype (PubMed:24373067, PubMed:22941047). Increased biofilm formation after 8 hours at 30 and 37 degrees Celsius, has risen higher by 24 hours at 37 degrees Celsius but has fallen by 24 hours at 30 degrees Celsius. Approximately 2-fold increase in swimming motility (PubMed:24373067). When single ghoT 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 metablbic rates (PubMed:24373067).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14F → A: Still digests ghoT RNA. 1 Publication1
Mutagenesisi15D → A: Still digests ghoT RNA. 1 Publication1
Mutagenesisi25L → I: Protein becomes toxic upon overexpression. Becomes classic type II TA toxin protein, increased cell persistence to ampicillin; when associated with L-31. 1 Publication1
Mutagenesisi26R → A: Slightly impaired digestion of ghoT RNA. 1 Publication1
Mutagenesisi28R → A: Reduced digestion of ghoT RNA, less efficient neutralization of GhoT in vivo. 1 Publication1
Mutagenesisi31M → L: Protein becomes toxic upon overexpression. Becomes classic type II TA toxin protein, increased cell persistence to ampicillin; when associated with I-25. 1 Publication1
Mutagenesisi55F → A: Reduced digestion of ghoT RNA. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001697331 – 98Endoribonuclease antitoxin GhoSAdd BLAST98

Post-translational modificationi

Unlike other TA proteinaceous antitoxins, this protein is stable with and without cellular stress; its structure has been determined in the absence of GhoT toxin.1 Publication

Proteomic databases

PaxDbiP0AF61
PRIDEiP0AF61

Expressioni

Inductioni

Post-transcriptionally down-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).1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4261767, 11 interactors
STRINGi316385.ECDH10B_4320

Structurei

Secondary structure

198
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 15Combined sources6
Helixi18 – 20Combined sources3
Helixi21 – 33Combined sources13
Beta strandi36 – 41Combined sources6
Beta strandi43 – 45Combined sources3
Beta strandi47 – 49Combined sources3
Beta strandi53 – 57Combined sources5
Helixi63 – 72Combined sources10
Helixi73 – 75Combined sources3
Beta strandi83 – 88Combined sources6
Helixi89 – 93Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LLZNMR-A1-98[»]
ProteinModelPortaliP0AF61
SMRiP0AF61
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000127074
KOiK18840
OMAiDDYFRQI

Family and domain databases

Gene3Di3.30.70.2360, 1 hit
InterProiView protein in InterPro
IPR022597 GhoS
IPR038241 GhoS_sf
PfamiView protein in Pfam
PF11080 GhoS, 1 hit

Sequencei

Sequence statusi: Complete.

P0AF61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGKNKFNTY VVSFDYPSSY SSVFLRLRSL MYDMNFSSIV ADEYGIPRQL
60 70 80 90
NENSFAITTS LAASEIEDLI RLKCLDLPDI DFDLNIMTVD DYFRQFYK
Length:98
Mass (Da):11,468
Last modified:December 20, 2005 - v1
Checksum:i8466741C8225E468
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA Translation: AAA97028.1
U00096 Genomic DNA Translation: AAC77089.1
AP009048 Genomic DNA Translation: BAE78130.1
PIRiS56357
RefSeqiNP_418552.1, NC_000913.3
WP_000398619.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC77089; AAC77089; b4128
BAE78130; BAE78130; BAE78130
GeneIDi948646
KEGGiecj:JW4089
eco:b4128
PATRICifig|511145.12.peg.4259

Similar proteinsi

Entry informationi

Entry nameiGHOS_ECOLI
AccessioniPrimary (citable) accession number: P0AF61
Secondary accession number(s): P39275, Q2M6H6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 28, 2018
This is version 74 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health