ID   ALLR_ECOL5              Reviewed;         271 AA.
AC   Q0TKD5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=HTH-type transcriptional repressor AllR;
DE   AltName: Full=Negative regulator of allantoin and glyoxylate utilization operons;
GN   Name=allR; OrderedLocusNames=ECP_0567;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG68596.1; -; Genomic_DNA.
DR   RefSeq; WP_000141275.1; NC_008253.1.
DR   AlphaFoldDB; Q0TKD5; -.
DR   SMR; Q0TKD5; -.
DR   STRING; 362663.ECP_0567; -.
DR   PRIDE; Q0TKD5; -.
DR   EnsemblBacteria; ABG68596; ABG68596; ECP_0567.
DR   GeneID; 67416416; -.
DR   KEGG; ecp:ECP_0567; -.
DR   HOGENOM; CLU_062618_7_1_6; -.
DR   OMA; DTTETIH; -.
DR   Proteomes; UP000009182; 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_0000313700"
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