TRER_SALTY
ID TRER_SALTY Reviewed; 315 AA.
AC P36674;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=HTH-type transcriptional regulator TreR {ECO:0000250|UniProtKB:P36673};
DE AltName: Full=Trehalose operon repressor {ECO:0000250|UniProtKB:P36673};
GN Name=treR; OrderedLocusNames=STM4455;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7751273; DOI=10.1128/jb.177.10.2654-2662.1995;
RA Tao T., Snavely M.D., Farr S.G., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: mgtA encodes a P-type
RT ATPase and is regulated by Mg2+ in a manner similar to that of the mgtB P-
RT type ATPase.";
RL J. Bacteriol. 177:2654-2662(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Repressor of the treBC operon. It is able to bind trehalose-
CC 6-phosphate. {ECO:0000250|UniProtKB:P36673}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P36673}.
CC -!- INDUCTION: Probably induced by trehalose-6-phosphate.
CC {ECO:0000250|UniProtKB:P36673}.
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DR EMBL; U07843; AAA68987.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23274.1; -; Genomic_DNA.
DR PIR; A57147; A57147.
DR RefSeq; NP_463315.1; NC_003197.2.
DR RefSeq; WP_001181297.1; NC_003197.2.
DR AlphaFoldDB; P36674; -.
DR SMR; P36674; -.
DR STRING; 99287.STM4455; -.
DR PaxDb; P36674; -.
DR EnsemblBacteria; AAL23274; AAL23274; STM4455.
DR GeneID; 1255981; -.
DR KEGG; stm:STM4455; -.
DR PATRIC; fig|99287.12.peg.4687; -.
DR HOGENOM; CLU_037628_9_0_6; -.
DR PhylomeDB; P36674; -.
DR BioCyc; SENT99287:STM4455-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0005991; P:trehalose metabolic process; IEA:InterPro.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR046335; LacI/GalR-like_sensor.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR012771; Trehalos_R_gpbac.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF13377; Peripla_BP_3; 1.
DR PRINTS; PR00036; HTHLACI.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR TIGRFAMs; TIGR02405; trehalos_R_Ecol; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..315
FT /note="HTH-type transcriptional regulator TreR"
FT /id="PRO_0000108006"
FT DOMAIN 5..59
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 7..26
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT BINDING 71..77
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000250|UniProtKB:P36673"
FT BINDING 126
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000250|UniProtKB:P36673"
FT BINDING 147
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000250|UniProtKB:P36673"
FT BINDING 187..190
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000250|UniProtKB:P36673"
FT BINDING 194
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000250|UniProtKB:P36673"
FT BINDING 242
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000250|UniProtKB:P36673"
FT BINDING 284
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000250|UniProtKB:P36673"
SQ SEQUENCE 315 AA; 34753 MW; 3115E6F0ADAC0E5A CRC64;
MQNRLTIKDI ARLSGVGKST VSRVLNNESG VSERTRERVE AVMNQHGFSP SRSARAMRGQ
SDKVVAIIVT RLDSLSENLA VQTMLPAFYE QGYDPIMMES QFSPTLVMEH LGMLRRRNID
GVVLFGFTGI TEELIAPWKA SLVLLARDAQ GFASVCYDDE GAIHILMQRL YEQGHRNISF
LGVPHSDITT GKRRHDAYLA FCKKHKLHPV AALPGLAMKQ GYEHTASVIM PDTTALVCAT
DTLALGASKY LQEQRIETLQ LASVGNTPLI KFLHPEIVTV DPGYAEAGRQ AASQLIEQIN
GRCDPRRIVI PSTLA
