ID   HIPB_ECOL6              Reviewed;          94 AA.
AC   Q8FHF3;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Antitoxin HipB;
GN   Name=hipB; OrderedLocusNames=c1941;
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 type II toxin-antitoxin (TA)
CC       system. Neutralizes the toxic effect of cognate toxin HipA. Represses
CC       the hipBA operon promoter (By similarity).
CC       {ECO:0000250|UniProtKB:P23873}.
CC   -!- SUBUNIT: Homodimer. Forms a HipA(2)HipB(2) heterotetramer which can
CC       interact with DNA. This complex also blocks the toxic activity of HipA
CC       (By similarity). {ECO:0000250|UniProtKB:P23873}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the hipB-hipA 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; AAN80399.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FHF3; -.
DR   SMR; Q8FHF3; -.
DR   STRING; 199310.c1941; -.
DR   EnsemblBacteria; AAN80399; AAN80399; c1941.
DR   KEGG; ecc:c1941; -.
DR   eggNOG; COG1396; Bacteria.
DR   HOGENOM; CLU_066192_47_2_6; -.
DR   OMA; HALEVHC; -.
DR   BioCyc; ECOL199310:C1941-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   Pfam; PF01381; HTH_3; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Repressor; Toxin-antitoxin system; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..94
FT                   /note="Antitoxin HipB"
FT                   /id="PRO_0000420797"
FT   DOMAIN          23..77
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DNA_BIND        34..53
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
SQ   SEQUENCE   94 AA;  10767 MW;  67F8EAD1F21837F4 CRC64;
     MLWTYDMMSF QKIYSPTQLA NAMKLVRQQN GWTQSELAKK IGIKQATISN FENNPDNTSL
     TTFFKILQSL ELSMTLCDAK NASPEAAEQQ DLEW