ID   ALLR_ECOK1              Reviewed;         271 AA.
AC   A1A8H2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=HTH-type transcriptional repressor AllR;
DE   AltName: Full=Negative regulator of allantoin and glyoxylate utilization operons;
GN   Name=allR; OrderedLocusNames=Ecok1_04680; ORFNames=APECO1_1508;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABI99961.1; -; Genomic_DNA.
DR   RefSeq; WP_000141274.1; NC_008563.1.
DR   AlphaFoldDB; A1A8H2; -.
DR   SMR; A1A8H2; -.
DR   EnsemblBacteria; ABI99961; ABI99961; APECO1_1508.
DR   KEGG; ecv:APECO1_1508; -.
DR   HOGENOM; CLU_062618_7_1_6; -.
DR   OMA; DTTETIH; -.
DR   Proteomes; UP000008216; 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; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..271
FT                   /note="HTH-type transcriptional repressor AllR"
FT                   /id="PRO_0000313699"
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;  29286 MW;  572F59EEC0F8308B 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 L