ID   MURR_ECOBR              Reviewed;         285 AA.
AC   C6UMS6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=ECB_02327;
OS   Escherichia coli (strain B / REL606).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=413997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / REL606;
RX   PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052;
RA   Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A.,
RA   Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B.,
RA   Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.;
RT   "Genome sequences of Escherichia coli B strains REL606 and BL21(DE3).";
RL   J. Mol. Biol. 394:644-652(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; CP000819; ACT39982.1; -; Genomic_DNA.
DR   RefSeq; WP_000966478.1; NC_012967.1.
DR   AlphaFoldDB; C6UMS6; -.
DR   SMR; C6UMS6; -.
DR   KEGG; ebr:ECB_02327; -.
DR   HOGENOM; CLU_055769_0_2_6; -.
DR   OMA; DHRIGSM; -.
DR   BioCyc; ECOL413997:GCQD-2541-MON; -.
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_0000387756"
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;  31283 MW;  A8619062407D4CE4 CRC64;
     MLYLTKISNA GSEFTENEQK IADFLRARVS ELKSVSSRQM AKQLGISQSS IVKFAQKLGA
     QGFTELRMAL IGEYSASREK TNATALHLHS SITSDDSLEV IARKLNREKE LALEQTCALF
     DYARLQKIID VISKAQFIQI TGLGGSALVG RDLSFKLMKI GYRVACEADT HVQATVSQAL
     KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLAD SPLRRLAHFT LDTVSGETEW
     RSSSMSTRTA QNSVTDLLFV GLVQLNDVES LKMIQRSSEL TQRLK