ID   MURR_ECOLC              Reviewed;         285 AA.
AC   B1IX45;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=EcolC_1252;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA76918.1; -; Genomic_DNA.
DR   RefSeq; WP_000966444.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IX45; -.
DR   SMR; B1IX45; -.
DR   KEGG; ecl:EcolC_1252; -.
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_0000387754"
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;  31395 MW;  51BDA412A0B51FA4 CRC64;
     MLYLTKIRNA ESEFTENEQK IADFLRANVS ELQSVSSRQM AKQLGISQSS IVKFAQKLGA
     QGFTELRMAL IGEYSASREK TNAMALHLHS SITSDDSLEV IARKLNREKE LALEQTCALF
     DYARLQKIIE VISKAPFIQI TGLGGSALVG RDLSFKLMKI GYRVACEADT HVQATVSQAL
     KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLAD SPLRRLAHFT LDTVSGETEW
     RSSSMSTRTA QNSVTDLLFV GLVQLNDVES LKMIQRSSEL TQRLK