ALLR_SALPA
ID ALLR_SALPA Reviewed; 272 AA.
AC Q5PCF5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=HTH-type transcriptional repressor AllR;
DE AltName: Full=Negative regulator of allantoin and glyoxylate utilization operons;
GN Name=allR; OrderedLocusNames=SPA2206;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV78093.1; -; Genomic_DNA.
DR RefSeq; WP_000141265.1; NC_006511.1.
DR AlphaFoldDB; Q5PCF5; -.
DR SMR; Q5PCF5; -.
DR EnsemblBacteria; AAV78093; AAV78093; SPA2206.
DR KEGG; spt:SPA2206; -.
DR HOGENOM; CLU_062618_7_1_6; -.
DR OMA; DTTETIH; -.
DR Proteomes; UP000008185; 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_0000313703"
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