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Protein

Endoribonuclease GhoS

Gene

ghoS

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

Functioni

Antitoxin component of a type V toxin-antitoxin (TA) module. 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

GO - Molecular functioni

  • endoribonuclease activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciEcoCyc:G7830-MONOMER.
ECOL316407:JW4089-MONOMER.
MetaCyc:G7830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoribonuclease 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141F → A: Still digests ghoT RNA. 1 Publication
Mutagenesisi15 – 151D → A: Still digests ghoT RNA. 1 Publication
Mutagenesisi25 – 251L → I: Protein becomes toxic upon overexpression. Becomes classic type II TA toxin protein, increased cell persistence to ampicillin; when associated with L-31. 1 Publication
Mutagenesisi26 – 261R → A: Slightly impaired digestion of ghoT RNA. 1 Publication
Mutagenesisi28 – 281R → A: Reduced digestion of ghoT RNA, less efficient neutralization of GhoT in vivo. 1 Publication
Mutagenesisi31 – 311M → L: Protein becomes toxic upon overexpression. Becomes classic type II TA toxin protein, increased cell persistence to ampicillin; when associated with I-25. 1 Publication
Mutagenesisi55 – 551F → A: Reduced digestion of ghoT RNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9898Endoribonuclease GhoSPRO_0000169733Add
BLAST

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.

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 interactions.
STRINGi511145.b4128.

Structurei

Secondary structure

1
98
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 156Combined sources
Helixi18 – 203Combined sources
Helixi21 – 3313Combined sources
Beta strandi36 – 416Combined sources
Beta strandi43 – 453Combined sources
Beta strandi47 – 493Combined sources
Beta strandi53 – 575Combined sources
Helixi63 – 7210Combined sources
Helixi73 – 753Combined sources
Beta strandi83 – 886Combined sources
Helixi89 – 935Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LLZNMR-A1-98[»]
ProteinModelPortaliP0AF61.
SMRiP0AF61. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000127074.
KOiK18840.
OMAiDDYFRQI.
OrthoDBiEOG6091GS.

Family and domain databases

InterProiIPR022597. GhoS.
[Graphical view]
PfamiPF11080. DUF2622. 1 hit.
[Graphical view]

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.

Genome annotation databases

EnsemblBacteriaiAAC77089; AAC77089; b4128.
BAE78130; BAE78130; BAE78130.
GeneIDi948646.
KEGGiecj:JW4089.
eco:b4128.
PATRICi32123821. VBIEscCol129921_4259.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LLZNMR-A1-98[»]
ProteinModelPortaliP0AF61.
SMRiP0AF61. Positions 1-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261767. 11 interactions.
STRINGi511145.b4128.

Proteomic databases

PaxDbiP0AF61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77089; AAC77089; b4128.
BAE78130; BAE78130; BAE78130.
GeneIDi948646.
KEGGiecj:JW4089.
eco:b4128.
PATRICi32123821. VBIEscCol129921_4259.

Organism-specific databases

EchoBASEiEB2361.
EcoGeneiEG12468. ghoS.

Phylogenomic databases

HOGENOMiHOG000127074.
KOiK18840.
OMAiDDYFRQI.
OrthoDBiEOG6091GS.

Enzyme and pathway databases

BioCyciEcoCyc:G7830-MONOMER.
ECOL316407:JW4089-MONOMER.
MetaCyc:G7830-MONOMER.

Miscellaneous databases

PROiP0AF61.

Family and domain databases

InterProiIPR022597. GhoS.
[Graphical view]
PfamiPF11080. DUF2622. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  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.
    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, DISRUPTION PHENOTYPE.
  6. "de novo synthesis of a bacterial toxin/antitoxin system."
    Soo V.W., Cheng H.Y., Kwan B.W., Wood T.K.
    Sci. Rep. 4:4807-4807(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-25 AND MET-31.
    Strain: K12 / BW25113.
  7. "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: STRUCTURE BY NMR, FUNCTION, SUBUNIT, PROTEIN STABILITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF PHE-14; ASP-15; ARG-26; ARG-28 AND PHE-55.
    Strain: K12 / BW25113.

Entry informationi

Entry nameiGHOS_ECOLI
AccessioniPrimary (citable) accession number: P0AF61
Secondary accession number(s): P39275, Q2M6H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 20, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.