RUTR_ECOL6
ID RUTR_ECOL6 Reviewed; 212 AA.
AC P0ACU3; P75899;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=HTH-type transcriptional regulator RutR;
DE AltName: Full=Rut operon repressor;
GN Name=rutR; OrderedLocusNames=c1150;
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: Master transcription regulator which represses the
CC degradation of pyrimidines (rutABCDEFG) and purines (gcl operon) for
CC maintenance of metabolic balance between pyrimidines and purines. It
CC also regulates the synthesis of pyrimidine nucleotides and arginine
CC from glutamine (carAB) and the supply of glutamate (gadABWX) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN79618.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN79618.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000191701.1; NC_004431.1.
DR AlphaFoldDB; P0ACU3; -.
DR SMR; P0ACU3; -.
DR STRING; 199310.c1150; -.
DR PRIDE; P0ACU3; -.
DR EnsemblBacteria; AAN79618; AAN79618; c1150.
DR GeneID; 60667996; -.
DR GeneID; 66670709; -.
DR KEGG; ecc:c1150; -.
DR eggNOG; COG1309; Bacteria.
DR HOGENOM; CLU_069356_1_0_6; -.
DR OMA; DPHHLIF; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001647; HTH_TetR.
DR InterPro; IPR036271; Tet_transcr_reg_TetR-rel_C_sf.
DR InterPro; IPR019915; Tscrpt_reg_pyr_util_RutR.
DR InterPro; IPR013573; Tscrpt_reg_YcdC_C.
DR Pfam; PF08362; TetR_C_3; 1.
DR Pfam; PF00440; TetR_N; 1.
DR PRINTS; PR00455; HTHTETR.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48498; SSF48498; 1.
DR TIGRFAMs; TIGR03613; RutR; 1.
DR PROSITE; PS50977; HTH_TETR_2; 1.
PE 3: Inferred from homology;
KW DNA-binding; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..212
FT /note="HTH-type transcriptional regulator RutR"
FT /id="PRO_0000070636"
FT DOMAIN 17..77
FT /note="HTH tetR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
FT DNA_BIND 39..58
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00335"
SQ SEQUENCE 212 AA; 23688 MW; E2459B85DFAC277A CRC64;
MTQGAVKTTG KRSRAVSAKK KAILSAALDT FSQFGFHGTR LEQIAELAGV SKTNLLYYFP
SKEALYIAVL RQILDIWLAP LKAFREDFAP LAAIKEYIRL KLEVSRDYPQ ASRLFCMEML
AGAPLLMDEL TGDLKALIDE KSALIAGWVK SGKLAPIDPQ HLIFMIWAST QHYADFAPQV
EAVTGATLRD EVFFNQTVEN VQRIIIEGIR PR