TRER_ECOLI
ID TRER_ECOLI Reviewed; 315 AA.
AC P36673; Q2M666;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=HTH-type transcriptional regulator TreR {ECO:0000303|PubMed:9148912};
DE AltName: Full=Trehalose operon repressor {ECO:0000303|PubMed:9148912};
GN Name=treR; OrderedLocusNames=b4241, JW4200;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=K12;
RX PubMed=9148912; DOI=10.1074/jbc.272.20.13026;
RA Horlacher R., Boos W.;
RT "Characterization of TreR, the major regulator of the Escherichia coli
RT trehalose system.";
RL J. Biol. Chem. 272:13026-13032(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 307-315, FUNCTION, DISRUPTION
RP PHENOTYPE, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=7608078; DOI=10.1128/jb.177.14.4043-4052.1995;
RA Klein W., Horlacher R., Boos W.;
RT "Molecular analysis of treB encoding the Escherichia coli enzyme II
RT specific for trehalose.";
RL J. Bacteriol. 177:4043-4052(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH
RP TREHALOSE-6-PHOSPHATE, AND SUBUNIT.
RX PubMed=9865945; DOI=10.1002/pro.5560071204;
RA Hars U., Horlacher R., Boos W., Welte W., Diederichs K.;
RT "Crystal structure of the effector-binding domain of the trehalose-
RT repressor of Escherichia coli, a member of the LacI family, in its
RT complexes with inducer trehalose-6-phosphate and noninducer trehalose.";
RL Protein Sci. 7:2511-2521(1998).
CC -!- FUNCTION: Repressor of the treBC operon. It is able to bind trehalose-
CC 6-phosphate and trehalose. {ECO:0000269|PubMed:7608078,
CC ECO:0000269|PubMed:9148912}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9148912,
CC ECO:0000269|PubMed:9865945}.
CC -!- INDUCTION: Probably induced by trehalose-6-phosphate.
CC {ECO:0000305|PubMed:7608078}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are constitutive in the
CC expression of the treBC operon. {ECO:0000269|PubMed:7608078}.
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DR EMBL; U07790; AAB47715.1; -; Unassigned_DNA.
DR EMBL; U14003; AAA97138.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77198.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78240.1; -; Genomic_DNA.
DR EMBL; U06195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S56467; S56467.
DR RefSeq; NP_418662.1; NC_000913.3.
DR RefSeq; WP_001181307.1; NZ_LN832404.1.
DR PDB; 4XXH; X-ray; 2.40 A; A/B=61-315.
DR PDBsum; 4XXH; -.
DR AlphaFoldDB; P36673; -.
DR SMR; P36673; -.
DR BioGRID; 4260956; 12.
DR BioGRID; 853049; 2.
DR DIP; DIP-11026N; -.
DR IntAct; P36673; 10.
DR STRING; 511145.b4241; -.
DR DrugBank; DB02430; Trehalose-6-Phosphate.
DR jPOST; P36673; -.
DR PaxDb; P36673; -.
DR PRIDE; P36673; -.
DR EnsemblBacteria; AAC77198; AAC77198; b4241.
DR EnsemblBacteria; BAE78240; BAE78240; BAE78240.
DR GeneID; 948760; -.
DR KEGG; ecj:JW4200; -.
DR KEGG; eco:b4241; -.
DR PATRIC; fig|1411691.4.peg.2460; -.
DR EchoBASE; EB2118; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_9_0_6; -.
DR OMA; HISFLGV; -.
DR PhylomeDB; P36673; -.
DR BioCyc; EcoCyc:EG12202-MON; -.
DR EvolutionaryTrace; P36673; -.
DR PRO; PR:P36673; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..315
FT /note="HTH-type transcriptional regulator TreR"
FT /id="PRO_0000108005"
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:0000269|PubMed:9865945"
FT BINDING 126
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000269|PubMed:9865945"
FT BINDING 147
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000269|PubMed:9865945"
FT BINDING 187..190
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000269|PubMed:9865945"
FT BINDING 194
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000269|PubMed:9865945"
FT BINDING 242
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000269|PubMed:9865945"
FT BINDING 284
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000269|PubMed:9865945"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4XXH"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4XXH"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4XXH"
FT HELIX 284..299
FT /evidence="ECO:0007829|PDB:4XXH"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4XXH"
SQ SEQUENCE 315 AA; 34531 MW; 16C528EBDE40C665 CRC64;
MQNRLTIKDI ARLSGVGKST VSRVLNNESG VSQLTRERVE AVMNQHGFSP SRSARAMRGQ
SDKVVAIIVT RLDSLSENLA VQTMLPAFYE QGYDPIMMES QFSPQLVAEH LGVLKRRNID
GVVLFGFTGI TEEMLAHWQS SLVLLARDAK GFASVCYDDE GAIKILMQRL YDQGHRNISY
LGVPHSDVTT GKRRHEAYLA FCKAHKLHPV AALPGLAMKQ GYENVAKVIT PETTALLCAT
DTLALGASKY LQEQRIDTLQ LASVGNTPLM KFLHPEIVTV DPGYAEAGRQ AACQLIAQVT
GRSEPQQIII PATLS
