ID   MURR_ECO5T              Reviewed;         285 AA.
AC   C6UQ16;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=HTH-type transcriptional regulator MurR {ECO:0000255|HAMAP-Rule:MF_02108};
DE   AltName: Full=MurPQ operon repressor {ECO:0000255|HAMAP-Rule:MF_02108};
GN   Name=murR {ECO:0000255|HAMAP-Rule:MF_02108}; OrderedLocusNames=ECSP_3374;
OS   Escherichia coli O157:H7 (strain TW14359 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=544404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW14359 / EHEC;
RX   PubMed=19564389; DOI=10.1128/iai.00198-09;
RA   Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C.,
RA   Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H.,
RA   Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K.,
RA   Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.;
RT   "Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-
RT   associated outbreak isolate indicates candidate genes that may enhance
RT   virulence.";
RL   Infect. Immun. 77:3713-3721(2009).
CC   -!- FUNCTION: Represses the expression of the murPQ operon involved in the
CC       uptake and degradation of N-acetylmuramic acid (MurNAc). Binds to two
CC       adjacent inverted repeats within the operator region. MurNAc 6-
CC       phosphate, the substrate of MurQ, is the specific inducer that weakens
CC       binding of MurR to the operator. {ECO:0000255|HAMAP-Rule:MF_02108}.
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation
CC       [regulation].
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_02108}.
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DR   EMBL; CP001368; ACT73141.1; -; Genomic_DNA.
DR   RefSeq; WP_000966443.1; NC_013008.1.
DR   AlphaFoldDB; C6UQ16; -.
DR   SMR; C6UQ16; -.
DR   KEGG; etw:ECSP_3374; -.
DR   HOGENOM; CLU_055769_0_2_6; -.
DR   OMA; DHRIGSM; -.
DR   UniPathway; UPA00342; -.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0043470; P:regulation of carbohydrate catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05013; SIS_RpiR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_02108; HTH_type_MurR; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR000281; HTH_RpiR.
DR   InterPro; IPR035472; RpiR-like_SIS.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR022821; Tscrpt_reg_HTH_MurR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01418; HTH_6; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   PROSITE; PS51071; HTH_RPIR; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; DNA-binding; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..285
FT                   /note="HTH-type transcriptional regulator MurR"
FT                   /id="PRO_0000387764"
FT   DOMAIN          1..77
FT                   /note="HTH rpiR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02108"
FT   DOMAIN          128..268
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02108"
FT   DNA_BIND        37..56
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02108"
SQ   SEQUENCE   285 AA;  31327 MW;  F61628D7F2016BC9 CRC64;
     MLYLTKIRNA ESEFTENEQK IADFLRANVS ELKSVSSRKM AKQLGISQSS IVKFAQKLGA
     QGFTELRMAL IGEYSASREK TNATAQHLHS SITSDDSLEV IARKLNREKE LALEQTCALF
     DYARLQKIIE VISKAPFIQI TGLGGSALVG CDLSFKLMKI GYRVACEADT HVQATVSQAL
     KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLAD SPLRRLAHFT LDTVSGETEW
     RSSSMSTRTA QNSVTDLLFV GLVQLNDVES LKMIQRSSEL TQRLK