GHOS_ECOLI
ID GHOS_ECOLI Reviewed; 98 AA.
AC P0AF61; P39275; Q2M6H6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Endoribonuclease antitoxin GhoS {ECO:0000303|PubMed:22941047};
DE EC=3.1.-.-;
DE AltName: Full=Antitoxin GhoS;
GN Name=ghoS {ECO:0000303|PubMed:22941047};
GN Synonyms=arT {ECO:0000303|PubMed:24797297}, yjdK;
GN OrderedLocusNames=b4128, JW4089;
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=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [3]
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 [4]
RP INDUCTION.
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, AND DISRUPTION PHENOTYPE.
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).
RN [6]
RP MUTAGENESIS OF LEU-25 AND MET-31.
RC STRAIN=K12 / BW25113;
RX PubMed=24797297; DOI=10.1038/srep04807;
RA Soo V.W., Cheng H.Y., Kwan B.W., Wood T.K.;
RT "de novo synthesis of a bacterial toxin/antitoxin system.";
RL Sci. Rep. 4:4807-4807(2014).
RN [7]
RP STRUCTURE BY NMR, FUNCTION, SUBUNIT, PROTEIN STABILITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF PHE-14; ASP-15; ARG-26; ARG-28 AND PHE-55.
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).
CC -!- FUNCTION: Antitoxin component of a type V toxin-antitoxin (TA) system.
CC Neutralizes the toxic effects of toxin GhoT by digesting ghoT
CC transcripts in a sequence-specific manner (PubMed:22941047). In concert
CC with GhoT is involved in reducing cell growth during antibacterial
CC stress (PubMed:24373067). Overexpression leads to transcript level
CC reduction of 20 other mRNAs involved in purine or pyrimidine synthesis
CC and transport. Not seen to bind its own promoter DNA (PubMed:22941047).
CC {ECO:0000269|PubMed:22941047, ECO:0000269|PubMed:24373067}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22941047}.
CC -!- INDUCTION: Post-transcriptionally down-regulated by MqsR which acts on
CC the ghoST transcript selectively, degrading the ghoS segment while
CC leaving ghoT intact; conditions which induce MqsR (e.g. overexpression,
CC nalidixic acid, azolocillin or H(2)O(2)) decrease ghoS expression and
CC thus increase ghoT transcripts (PubMed:23289863).
CC {ECO:0000269|PubMed:23289863}.
CC -!- PTM: Unlike other TA proteinaceous antitoxins, this protein is stable
CC with and without cellular stress; its structure has been determined in
CC the absence of GhoT toxin. {ECO:0000269|PubMed:22941047}.
CC -!- DISRUPTION PHENOTYPE: Essential; cannot be disrupted unless ghoT is
CC also disrupted; in the double ghoS-ghoT mutant has no visible phenotype
CC (PubMed:24373067, PubMed:22941047). Increased biofilm formation after 8
CC hours at 30 and 37 degrees Celsius, has risen higher by 24 hours at 37
CC degrees Celsius but has fallen by 24 hours at 30 degrees Celsius.
CC Approximately 2-fold increase in swimming motility (PubMed:24373067).
CC When single ghoT mutant is grown in the presence of antibiotics
CC carbenicillin or cefoxitin initial metabolism is significantly
CC increased over that of wild-type, after 14 hours wild-type is slightly
CC less active. In a double ghoS-ghoT mutant in presence of the 2
CC antibiotics metabolism is significantly increased over that of wild-
CC type, but by 9 hours wild-type has caught up and eventually has
CC slightly greater metabolic rates (PubMed:24373067).
CC {ECO:0000269|PubMed:22941047, ECO:0000269|PubMed:24373067}.
CC -!- MISCELLANEOUS: Has a similar 3D-structure to Cas2 proteins.
CC {ECO:0000269|PubMed:22941047}.
CC -!- MISCELLANEOUS: Can be modified to become a classic type II TA toxin
CC (called ArT) which causes cells to become ghost-like, probably by
CC broadening substrate RNA recognition; the toxic activity is independent
CC of ghoT and mqsRA. Antitoxins to this evolved ArT toxin have been
CC artificially evolved from antitoxins mqsA (a type II TA system) and
CC toxI (a type I TA system). {ECO:0000269|PubMed:24797297}.
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DR EMBL; U14003; AAA97028.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77089.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78130.1; -; Genomic_DNA.
DR PIR; S56357; S56357.
DR RefSeq; NP_418552.1; NC_000913.3.
DR RefSeq; WP_000398619.1; NZ_SSZK01000018.1.
DR PDB; 2LLZ; NMR; -; A=1-98.
DR PDBsum; 2LLZ; -.
DR AlphaFoldDB; P0AF61; -.
DR BMRB; P0AF61; -.
DR SMR; P0AF61; -.
DR BioGRID; 4261767; 11.
DR STRING; 511145.b4128; -.
DR jPOST; P0AF61; -.
DR PaxDb; P0AF61; -.
DR PRIDE; P0AF61; -.
DR EnsemblBacteria; AAC77089; AAC77089; b4128.
DR EnsemblBacteria; BAE78130; BAE78130; BAE78130.
DR GeneID; 66671961; -.
DR GeneID; 948646; -.
DR KEGG; ecj:JW4089; -.
DR KEGG; eco:b4128; -.
DR PATRIC; fig|511145.12.peg.4259; -.
DR EchoBASE; EB2361; -.
DR HOGENOM; CLU_182150_0_0_6; -.
DR OMA; DDYFRQI; -.
DR BioCyc; EcoCyc:G7830-MON; -.
DR BioCyc; MetaCyc:G7830-MON; -.
DR PRO; PR:P0AF61; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:EcoCyc.
DR Gene3D; 3.30.70.2360; -; 1.
DR InterPro; IPR022597; GhoS.
DR InterPro; IPR038241; GhoS_sf.
DR Pfam; PF11080; GhoS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..98
FT /note="Endoribonuclease antitoxin GhoS"
FT /id="PRO_0000169733"
FT MUTAGEN 14
FT /note="F->A: Still digests ghoT RNA."
FT /evidence="ECO:0000269|PubMed:22941047"
FT MUTAGEN 15
FT /note="D->A: Still digests ghoT RNA."
FT /evidence="ECO:0000269|PubMed:22941047"
FT MUTAGEN 25
FT /note="L->I: Protein becomes toxic upon overexpression.
FT Becomes classic type II TA toxin protein, increased cell
FT persistence to ampicillin; when associated with L-31."
FT /evidence="ECO:0000269|PubMed:24797297"
FT MUTAGEN 26
FT /note="R->A: Slightly impaired digestion of ghoT RNA."
FT /evidence="ECO:0000269|PubMed:22941047"
FT MUTAGEN 28
FT /note="R->A: Reduced digestion of ghoT RNA, less efficient
FT neutralization of GhoT in vivo."
FT /evidence="ECO:0000269|PubMed:22941047"
FT MUTAGEN 31
FT /note="M->L: Protein becomes toxic upon overexpression.
FT Becomes classic type II TA toxin protein, increased cell
FT persistence to ampicillin; when associated with I-25."
FT /evidence="ECO:0000269|PubMed:24797297"
FT MUTAGEN 55
FT /note="F->A: Reduced digestion of ghoT RNA."
FT /evidence="ECO:0000269|PubMed:22941047"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2LLZ"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2LLZ"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:2LLZ"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2LLZ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2LLZ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2LLZ"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2LLZ"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:2LLZ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2LLZ"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2LLZ"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:2LLZ"
SQ SEQUENCE 98 AA; 11468 MW; 8466741C8225E468 CRC64;
MEGKNKFNTY VVSFDYPSSY SSVFLRLRSL MYDMNFSSIV ADEYGIPRQL NENSFAITTS
LAASEIEDLI RLKCLDLPDI DFDLNIMTVD DYFRQFYK
