ALLR_SALCH
ID ALLR_SALCH Reviewed; 272 AA.
AC Q57S48;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, 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=SCH_0557;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX64463.1; -; Genomic_DNA.
DR RefSeq; WP_000141265.1; NC_006905.1.
DR AlphaFoldDB; Q57S48; -.
DR SMR; Q57S48; -.
DR EnsemblBacteria; AAX64463; AAX64463; SCH_0557.
DR KEGG; sec:SCH_0557; -.
DR HOGENOM; CLU_062618_7_1_6; -.
DR OMA; DTTETIH; -.
DR Proteomes; UP000000538; 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..272
FT /note="HTH-type transcriptional repressor AllR"
FT /id="PRO_0000313702"
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 REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 272 AA; 29219 MW; EAFC0B2B1463DD75 CRC64;
MTEVRRRGRP GQAEPTAQKG AQALERGIAI LQYLERSGGS SSVSDISGSL DLPLSTTFRL
LKVLQAADFV YQDSQLGWWH IGLGVFNVGS AYIHNRDVLS VAGPFMHRLM LLSGETVNVA
IRNGNEAVLI GQKECKSMVR MCAPLGSRLP LHASGAGKAL LYPLTEEELV GIVVNTGLRR
FTPTTLVDLP ILLKNLEQAR EQGYTVDQEE HVVGLNCIAS AIYDDAGSVV AAISISGPAS
RLTEDRFISQ GELVRDTAKD ISTALGLKPP VA