ALLR_ECOL6
ID ALLR_ECOL6 Reviewed; 271 AA.
AC P0ACN5; P77734;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=HTH-type transcriptional repressor AllR;
DE AltName: Full=Negative regulator of allantoin and glyoxylate utilization operons;
GN Name=allR; OrderedLocusNames=c0621;
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).
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; AE014075; AAN79098.1; -; Genomic_DNA.
DR RefSeq; WP_000141275.1; NC_004431.1.
DR AlphaFoldDB; P0ACN5; -.
DR SMR; P0ACN5; -.
DR STRING; 199310.c0621; -.
DR EnsemblBacteria; AAN79098; AAN79098; c0621.
DR GeneID; 67416416; -.
DR KEGG; ecc:c0621; -.
DR eggNOG; COG1414; Bacteria.
DR HOGENOM; CLU_062618_7_1_6; -.
DR OMA; DTTETIH; -.
DR BioCyc; ECOL199310:C0621-MON; -.
DR Proteomes; UP000001410; 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_0000201755"
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