GNTR_ECOL6
ID GNTR_ECOL6 Reviewed; 331 AA.
AC P0ACP6; P46860; Q47241;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=HTH-type transcriptional regulator GntR;
DE AltName: Full=Gluconate utilization system GNT-I transcriptional repressor;
GN Name=gntR; OrderedLocusNames=c4227;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Negative regulator for the gluconate utilization system GNT-
CC I, the gntUKR operon. {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation
CC [regulation].
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DR EMBL; AE014075; AAN82665.1; -; Genomic_DNA.
DR RefSeq; WP_000730252.1; NC_004431.1.
DR AlphaFoldDB; P0ACP6; -.
DR SMR; P0ACP6; -.
DR STRING; 199310.c4227; -.
DR EnsemblBacteria; AAN82665; AAN82665; c4227.
DR GeneID; 60902224; -.
DR KEGG; ecc:c4227; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_3_6; -.
DR OMA; MVFVDRW; -.
DR BioCyc; ECOL199310:C4227-MON; -.
DR UniPathway; UPA00792; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR001761; Peripla_BP/Lac1_sug-bd_dom.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF00532; Peripla_BP_1; 1.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..331
FT /note="HTH-type transcriptional regulator GntR"
FT /id="PRO_0000107959"
FT DOMAIN 6..60
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 8..27
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
SQ SEQUENCE 331 AA; 36422 MW; 5A40666364E0C896 CRC64;
MKKKRPVLQD VADRVGVTKM TVSRFLRNPE QVSVALRGKI AAALDELGYI PNRAPDILSN
ATSRAIGVLL PSLTNQVFAE VLRGIESVTD AHGYQTMLAH YGYKPEMEQE RLESMLSWNI
DGLILTERTH TPRTLKMIEV AGIPVVELMD SKSPCLDIAV GFDNFEAARQ MTTAIIARGH
RHIAYLGARL DERTIIKQKG YEQAMLDAGL VPYSVMVEQS SSYSSGIELI RQARREYPQL
DGVFCTNDDL AVGAAFECQR LGLKVPDDMA IAGFHGHDIG QVMEPRLASV LTPRERMGSI
GAERLLARIR GESVTPKMLD LGFTLSPGGS I