ID   MURR_SHIB3              Reviewed;         285 AA.
AC   B2TX16;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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};
GN   OrderedLocusNames=SbBS512_E2799;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-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; CP001063; ACD08176.1; -; Genomic_DNA.
DR   RefSeq; WP_000966474.1; NC_010658.1.
DR   AlphaFoldDB; B2TX16; -.
DR   SMR; B2TX16; -.
DR   STRING; 344609.SbBS512_E2799; -.
DR   EnsemblBacteria; ACD08176; ACD08176; SbBS512_E2799.
DR   KEGG; sbc:SbBS512_E2799; -.
DR   HOGENOM; CLU_055769_0_2_6; -.
DR   OMA; DHRIGSM; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000001030; Chromosome.
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_0000387771"
FT   DOMAIN          1..77
FT                   /note="HTH rpiR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02108"
FT   DOMAIN          128..279
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;  31168 MW;  E031B0995A14B134 CRC64;
     MLYLTKISNA GSEFTENEQK IADFLQANVS ELQSVSSRQM AKQLGISQSS IVKFAQKLGA
     QGFTELRMAL IGEYSASREK TNTTALHLHS SITSDDSLEV IARKLNREKE LALEQTCALF
     DYARLQKIIE VISKAPFIQI TGLGGSALVG RDLSFKLMKI GYRVACEADT HVQATVSQAL
     KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLAD SPLRRLAHFT LDTVSGETEW
     RSSSMSTRTA QNSVTDLLFV GLVQLNDVAS LKMIQRSSEL TQRLK