(data stored in ACNUC7421 zone)

SWISSPROT: ALLR_ECO57

ID   ALLR_ECO57              Reviewed;         271 AA.
AC   P0ACN6; P77734;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 77.
DE   RecName: Full=HTH-type transcriptional repressor AllR;
DE   AltName: Full=Negative regulator of allantoin and glyoxylate utilization operons;
GN   Name=allR; OrderedLocusNames=Z0660, ECs0567;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Negative regulator of allantoin and glyoxylate
CC       utilization operons. Binds to the gcl promoter and to the allS-
CC       allA intergenic region (By similarity). {ECO:0000250}.
DR   EMBL; AE005174; AAG54862.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33990.1; -; Genomic_DNA.
DR   PIR; B85550; B85550.
DR   PIR; G90699; G90699.
DR   RefSeq; NP_308594.1; NC_002695.1.
DR   RefSeq; WP_000141275.1; NZ_MWVM01000032.1.
DR   ProteinModelPortal; P0ACN6; -.
DR   SMR; P0ACN6; -.
DR   STRING; 155864.Z0660; -.
DR   PRIDE; P0ACN6; -.
DR   EnsemblBacteria; AAG54862; AAG54862; Z0660.
DR   EnsemblBacteria; BAB33990; BAB33990; BAB33990.
DR   GeneID; 915706; -.
DR   KEGG; ece:Z0660; -.
DR   KEGG; ecs:ECs0567; -.
DR   PATRIC; fig|386585.9.peg.675; -.
DR   eggNOG; ENOG4108N16; Bacteria.
DR   eggNOG; COG1414; LUCA.
DR   HOGENOM; HOG000107041; -.
DR   KO; K10973; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   InterPro; IPR029016; GAF_dom-like.
DR   InterPro; IPR014757; Tscrpt_reg_IclR_C.
DR   InterPro; IPR005471; Tscrpt_reg_IclR_N.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   Pfam; PF09339; HTH_IclR; 1.
DR   Pfam; PF01614; IclR; 1.
DR   SMART; SM00346; HTH_ICLR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF55781; SSF55781; 1.
DR   PROSITE; PS51077; HTH_ICLR; 1.
DR   PROSITE; PS51078; ICLR_ED; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0ACN6.
DR   SWISS-2DPAGE; P0ACN6.
KW   Complete proteome; DNA-binding; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    271       HTH-type transcriptional repressor AllR.
FT                                /FTId=PRO_0000201754.
FT   DOMAIN       21     83       HTH iclR-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00393}.
FT   DOMAIN       98    267       IclR-ED. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00394}.
FT   DNA_BIND     43     62       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00393}.
FT   REGION      154    156       Glyoxylate binding. {ECO:0000250}.
FT   REGION      234    236       Glyoxylate binding. {ECO:0000250}.
FT   BINDING     207    207       Glyoxylate. {ECO:0000250}.
FT   BINDING     217    217       Glyoxylate. {ECO:0000250}.
SQ   SEQUENCE   271 AA;  29270 MW;  476F59EEC0F8308B CRC64;
     MTEVRRRGRP GQAEPVAQKG AQALERGIAI LQYLEKSGGS SSVSDISLNL DLPLSTTFRL
     LKVLQAADFV YQDSQLGWWH IGLGVFNVGA AYIHNRDVLS VAGPFMRRLM LLSGETVNVA
     IRNGNEAVLI GQLECKSMVR MCAPLGSRLP LHASGAGKAL LYPLAEEELM SIILQTGLQQ
     FTPTTLVDMP TLLKDLEQAR ELGYTVDKEE HVVGLNCIAS AIYDDVGSVV AAISISGPSS
     RLTEDRFVSQ GELVRDTARD ISTALGLKAH P
//

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