PRLF_ECOL6
ID PRLF_ECOL6 Reviewed; 111 AA.
AC Q8FDB5;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Antitoxin PrlF;
GN Name=prlF; Synonyms=sohA; OrderedLocusNames=c3884;
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: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Labile antitoxin that binds to the YhaV toxin and neutralizes its
CC ribonuclease activity. Also acts as a transcription factor. The
CC YhaV/PrlF complex binds the prlF-yhaV operon, probably negatively
CC regulating its expression (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; forms a complex with YhaV with stoichiometry
CC PrlF(2)-YhaV(4), possibly as a YhaV(2)-PrlF(2)-YhaV(2) complex like the
CC MazFE complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; AAN82325.1; -; Genomic_DNA.
DR RefSeq; WP_001296435.1; NC_004431.1.
DR AlphaFoldDB; Q8FDB5; -.
DR STRING; 199310.c3884; -.
DR EnsemblBacteria; AAN82325; AAN82325; c3884.
DR GeneID; 66506893; -.
DR KEGG; ecc:c3884; -.
DR eggNOG; COG2002; Bacteria.
DR HOGENOM; CLU_143957_0_0_6; -.
DR OMA; DKICYTI; -.
DR BioCyc; ECOL199310:C3884-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0097351; F:toxin sequestering activity; IEA:InterPro.
DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR InterPro; IPR031848; PrlF_antitoxin.
DR InterPro; IPR007159; SpoVT-AbrB_dom.
DR InterPro; IPR037914; SpoVT-AbrB_sf.
DR Pfam; PF15937; PrlF_antitoxin; 1.
DR SUPFAM; SSF89447; SSF89447; 1.
DR PROSITE; PS51740; SPOVT_ABRB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-binding; Repressor; Toxin-antitoxin system; Transcription;
KW Transcription regulation.
FT CHAIN 1..111
FT /note="Antitoxin PrlF"
FT /id="PRO_0000420798"
FT DOMAIN 12..59
FT /note="SpoVT-AbrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
SQ SEQUENCE 111 AA; 12322 MW; 85201B7B093E2382 CRC64;
MPANARSNAV LTTESKVTIR GQTTIPAPVR EALKLKPGLD SIHYEILPGG QVFMCRLGDE
QEDHTMNAFL RFLDADIQNN PQKTRPFDIQ QGKKLVAGMD VNIDDEIGDD E