ID   ALLR_ECO57              Reviewed;         271 AA.
AC   P0ACN6; P77734;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=HTH-type transcriptional repressor AllR;
DE   AltName: Full=Negative regulator of allantoin and glyoxylate utilization operons;
GN   Name=allR; OrderedLocusNames=Z0660, ECs0567;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Negative regulator of allantoin and glyoxylate utilization
CC       operons. Binds to the gcl promoter and to the allS-allA intergenic
CC       region (By similarity). {ECO:0000250}.
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DR   EMBL; AE005174; AAG54862.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33990.1; -; Genomic_DNA.
DR   PIR; B85550; B85550.
DR   PIR; G90699; G90699.
DR   RefSeq; NP_308594.1; NC_002695.1.
DR   RefSeq; WP_000141275.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0ACN6; -.
DR   SMR; P0ACN6; -.
DR   STRING; 155864.EDL933_0591; -.
DR   EnsemblBacteria; AAG54862; AAG54862; Z0660.
DR   EnsemblBacteria; BAB33990; BAB33990; ECs_0567.
DR   GeneID; 67416416; -.
DR   GeneID; 915706; -.
DR   KEGG; ece:Z0660; -.
DR   KEGG; ecs:ECs_0567; -.
DR   PATRIC; fig|386585.9.peg.675; -.
DR   eggNOG; COG1414; Bacteria.
DR   HOGENOM; CLU_062618_7_1_6; -.
DR   OMA; DTTETIH; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR014757; Tscrpt_reg_IclR_C.
DR   InterPro; IPR005471; Tscrpt_reg_IclR_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF09339; HTH_IclR; 1.
DR   Pfam; PF01614; IclR; 1.
DR   SMART; SM00346; HTH_ICLR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51077; HTH_ICLR; 1.
DR   PROSITE; PS51078; ICLR_ED; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..271
FT                   /note="HTH-type transcriptional repressor AllR"
FT                   /id="PRO_0000201754"
FT   DOMAIN          21..83
FT                   /note="HTH iclR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   DOMAIN          98..267
FT                   /note="IclR-ED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00394"
FT   DNA_BIND        43..62
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   BINDING         154..156
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250"
FT   BINDING         234..236
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   271 AA;  29270 MW;  476F59EEC0F8308B CRC64;
     MTEVRRRGRP GQAEPVAQKG AQALERGIAI LQYLEKSGGS SSVSDISLNL DLPLSTTFRL
     LKVLQAADFV YQDSQLGWWH IGLGVFNVGA AYIHNRDVLS VAGPFMRRLM LLSGETVNVA
     IRNGNEAVLI GQLECKSMVR MCAPLGSRLP LHASGAGKAL LYPLAEEELM SIILQTGLQQ
     FTPTTLVDMP TLLKDLEQAR ELGYTVDKEE HVVGLNCIAS AIYDDVGSVV AAISISGPSS
     RLTEDRFVSQ GELVRDTARD ISTALGLKAH P