ID   ALLR_SALTI              Reviewed;         272 AA.
AC   Q8Z8R2; Q7C8C8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=HTH-type transcriptional repressor AllR;
DE   AltName: Full=Negative regulator of allantoin and glyoxylate utilization operons;
GN   Name=allR; Synonyms=glxA3; OrderedLocusNames=STY0564, t2344;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AE014613; AAO69937.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD05001.1; -; Genomic_DNA.
DR   RefSeq; NP_455110.1; NC_003198.1.
DR   RefSeq; WP_000141266.1; NZ_WSUR01000008.1.
DR   AlphaFoldDB; Q8Z8R2; -.
DR   SMR; Q8Z8R2; -.
DR   STRING; 220341.16501785; -.
DR   PRIDE; Q8Z8R2; -.
DR   EnsemblBacteria; AAO69937; AAO69937; t2344.
DR   KEGG; stt:t2344; -.
DR   KEGG; sty:STY0564; -.
DR   PATRIC; fig|220341.7.peg.566; -.
DR   eggNOG; COG1414; Bacteria.
DR   HOGENOM; CLU_062618_7_1_6; -.
DR   OMA; DTTETIH; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000313704"
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;  29248 MW;  EAFC08E7DB6011BA CRC64;
     MTEVRRRGRP GQAEPTAQKG AQALERGIAI LQYLERSGGS SSVSDISGSL DLPLSTTFRL
     LKVLQAADFV YQDSQLGWWH IGLGVFNVGS AYIHNRDVLS VAGPFMHRLM LLSGETVNVA
     IRNGNEAVLI GQKECKSMVR MCAPLGSRLP LHASGAGKAL LYPLTEEELV GIVVNTGLRR
     FTPTTLVDLP ILLKNLERAR EQGYTVDQEE HVVGLNCIAS AIYDDAGSVV AAISISGPAS
     RLTEDRFISQ GELVRDTAKD ISTALGLKPP VA