ALLR_ECOUT
ID ALLR_ECOUT Reviewed; 271 AA.
AC Q1RF28;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=HTH-type transcriptional repressor AllR;
DE AltName: Full=Negative regulator of allantoin and glyoxylate utilization operons;
GN Name=allR; OrderedLocusNames=UTI89_C0535;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE06036.1; -; Genomic_DNA.
DR RefSeq; WP_000141274.1; NC_007946.1.
DR AlphaFoldDB; Q1RF28; -.
DR SMR; Q1RF28; -.
DR EnsemblBacteria; ABE06036; ABE06036; UTI89_C0535.
DR KEGG; eci:UTI89_C0535; -.
DR HOGENOM; CLU_062618_7_1_6; -.
DR OMA; DTTETIH; -.
DR Proteomes; UP000001952; 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_0000313698"
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
