YHAV_ECOL6
ID YHAV_ECOL6 Reviewed; 154 AA.
AC Q8FDB4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Toxin YhaV;
DE EC=3.1.-.-;
DE AltName: Full=Ribonuclease YhaV;
GN Name=yhaV; OrderedLocusNames=c3885;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=23055930; DOI=10.1371/journal.ppat.1002954;
RA Norton J.P., Mulvey M.A.;
RT "Toxin-antitoxin systems are important for niche-specific colonization and
RT stress resistance of uropathogenic Escherichia coli.";
RL PLoS Pathog. 8:E1002954-E1002954(2012).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has
CC RNase activity in vitro. Acts as a transcription factor. The YhaV/PrlF
CC complex binds the prlF-yhaV operon, probably negatively regulating its
CC expression (By similarity). {ECO:0000250}.
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. May dimerize in solution (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the prlF-yhaV operon has no effect on
CC virulence in mouse infection; the disrupted strain is as virulent as
CC wild-type. {ECO:0000269|PubMed:23055930}.
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DR EMBL; AE014075; AAN82326.1; -; Genomic_DNA.
DR RefSeq; WP_000347252.1; NC_004431.1.
DR AlphaFoldDB; Q8FDB4; -.
DR SMR; Q8FDB4; -.
DR STRING; 199310.c3885; -.
DR EnsemblBacteria; AAN82326; AAN82326; c3885.
DR KEGG; ecc:c3885; -.
DR eggNOG; ENOG502ZB6Z; Bacteria.
DR HOGENOM; CLU_137758_0_0_6; -.
DR OMA; MQRHGWT; -.
DR BioCyc; ECOL199310:C3885-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR InterPro; IPR021679; Toxin_endonuclease_YhaV.
DR Pfam; PF11663; Toxin_YhaV; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; Repressor; Toxin-antitoxin system;
KW Transcription; Transcription regulation.
FT CHAIN 1..154
FT /note="Toxin YhaV"
FT /id="PRO_0000420799"
SQ SEQUENCE 154 AA; 17750 MW; 7590078B13276BB2 CRC64;
MDFPQRVNGW ALYAHPCFQE TYDALVAEVE ALKGKDPENY QRKAATKLLA VVHKVIEEHI
TVNPSSPAFR HGKSLGSGKN KDWSRVKFGA GRYRLFFRYS EKEKVIILGW MNDENTLRTY
GKKTDAYTVF SKMLKRGHPP ADWESLTQET EESH