YHAV_ECOLI
ID YHAV_ECOLI Reviewed; 154 AA.
AC P64594; P42901; Q2M979;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ribonuclease toxin YhaV;
DE EC=3.1.-.-;
DE AltName: Full=Ribonuclease YhaV;
GN Name=yhaV; OrderedLocusNames=b3130, JW3099;
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=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 [2]
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 [3]
RP FUNCTION AS A TOXIN, FUNCTION AS A RIBONUCLEASE, SUBUNIT, MUTAGENESIS OF
RP ARG-85; 85-ARG--ARG-94 AND ARG-94, AND OPERON STRUCTURE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=17706670; DOI=10.1016/j.jmb.2007.07.016;
RA Schmidt O., Schuenemann V.J., Hand N.J., Silhavy T.J., Martin J.,
RA Lupas A.N., Djuranovic S.;
RT "prlF and yhaV encode a new toxin-antitoxin system in Escherichia coli.";
RL J. Mol. Biol. 372:894-905(2007).
RN [4]
RP REVIEW.
RX PubMed=19215780; DOI=10.1016/s0079-6603(08)00812-x;
RA Yamaguchi Y., Inouye M.;
RT "mRNA interferases, sequence-specific endoribonucleases from the toxin-
RT antitoxin systems.";
RL Prog. Mol. Biol. Transl. Sci. 85:467-500(2009).
RN [5]
RP RETRACTED PAPER.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21788497; DOI=10.1073/pnas.1100186108;
RA Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
RT "Bacterial persistence by RNA endonucleases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13206-13211(2011).
RN [6]
RP RETRACTION NOTICE OF PUBMED:21788497.
RX PubMed=29531044; DOI=10.1073/pnas.1803278115;
RA Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2901-E2901(2018).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has
CC RNase activity in vitro. Overexpression leads to growth arrest after 30
CC minutes; these effects are overcome by concomitant expression of
CC antitoxin SohA (PrlF). Massive overexpression is toxic. Unlike most
CC other characterized TA systems degrades rRNA, and co-folding of the
CC both TA proteins is necessary in vitro for inhibition of the RNase
CC activity. It is not known if it has any sequence-specificity. Acts as a
CC transcription factor. The YhaV/PrlF complex binds the prlF-yhaV operon,
CC probably negatively regulating its expression.
CC {ECO:0000269|PubMed:17706670}.
CC -!- SUBUNIT: Homohexamer; forms a complex with PrlF (SohA) with
CC stoichiometry PrlF(2)-YhaV(4), possibly as a YhaV(2)-PrlF(2)-YhaV(2)
CC complex like the MazFE complex. This complex is seen to dimerize in
CC solution. {ECO:0000269|PubMed:17706670}.
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DR EMBL; U18997; AAA57933.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76164.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77177.1; -; Genomic_DNA.
DR PIR; F65102; F65102.
DR RefSeq; NP_417599.1; NC_000913.3.
DR RefSeq; WP_000347273.1; NZ_LN832404.1.
DR AlphaFoldDB; P64594; -.
DR SMR; P64594; -.
DR BioGRID; 4262413; 9.
DR ComplexPortal; CPX-4102; PrlF-YhaV toxin-antitoxin complex.
DR STRING; 511145.b3130; -.
DR jPOST; P64594; -.
DR PaxDb; P64594; -.
DR PRIDE; P64594; -.
DR EnsemblBacteria; AAC76164; AAC76164; b3130.
DR EnsemblBacteria; BAE77177; BAE77177; BAE77177.
DR GeneID; 947638; -.
DR KEGG; ecj:JW3099; -.
DR KEGG; eco:b3130; -.
DR PATRIC; fig|1411691.4.peg.3601; -.
DR EchoBASE; EB2614; -.
DR eggNOG; ENOG502ZB6Z; Bacteria.
DR HOGENOM; CLU_137758_0_0_6; -.
DR InParanoid; P64594; -.
DR OMA; MQRHGWT; -.
DR PhylomeDB; P64594; -.
DR BioCyc; EcoCyc:G7629-MON; -.
DR BioCyc; MetaCyc:G7629-MON; -.
DR PRO; PR:P64594; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IPI:ComplexPortal.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:EcoCyc.
DR GO; GO:0004540; F:ribonuclease activity; IDA:EcoCyc.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:EcoCyc.
DR GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:EcoCyc.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:EcoCyc.
DR GO; GO:0044010; P:single-species biofilm formation; IDA:ComplexPortal.
DR InterPro; IPR021679; Toxin_endonuclease_YhaV.
DR Pfam; PF11663; Toxin_YhaV; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Nuclease; Reference proteome; Repressor;
KW Toxin-antitoxin system; Transcription; Transcription regulation.
FT CHAIN 1..154
FT /note="Ribonuclease toxin YhaV"
FT /id="PRO_0000169450"
FT MUTAGEN 85..94
FT /note="RVKFGAGRYR->AVKFGAGRYA: Complete loss of toxicity."
FT /evidence="ECO:0000269|PubMed:17706670"
FT MUTAGEN 85
FT /note="R->A: Partial loss of toxicity."
FT /evidence="ECO:0000269|PubMed:17706670"
FT MUTAGEN 94
FT /note="R->A: Partial loss of toxicity."
FT /evidence="ECO:0000269|PubMed:17706670"
SQ SEQUENCE 154 AA; 17836 MW; 758EBC8263326962 CRC64;
MDFPQRVNGW ALYAHPCFQE TYDALVAEVE TLKGKDPENY QRKAATKLLA VVHKVIEEHI
TVNPSSPAFR HGKSLGSGKN KDWSRVKFGA GRYRLFFRYS EKEKVIILGW MNDENTLRTY
GKKTDAYTVF SKMLKRGHPP ADWETLTRET EETH
