ID   MURR_SHIF8              Reviewed;         266 AA.
AC   Q0T281;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=SFV_2480;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF04584.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0T281; -.
DR   SMR; Q0T281; -.
DR   EnsemblBacteria; ABF04584; ABF04584; SFV_2480.
DR   KEGG; sfv:SFV_2480; -.
DR   HOGENOM; CLU_055769_0_2_6; -.
DR   OMA; DHRIGSM; -.
DR   UniPathway; UPA00342; -.
DR   Proteomes; UP000000659; 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..266
FT                   /note="HTH-type transcriptional regulator MurR"
FT                   /id="PRO_0000387775"
FT   DOMAIN          1..77
FT                   /note="HTH rpiR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02108"
FT   DOMAIN          128..266
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   266 AA;  29129 MW;  20858D13DF6298F6 CRC64;
     MLYLTKIRNA ESEFTGNEQK IADFLRARVS ELKSVSSRQM AKQLGISQSS IVKFAQKLGA
     QGFTELRMAL IGEYSASREK TNATALHLHS SITSDDSLEV IARKLNREKE LALEQTCALF
     DYARLQKIIE VISKAPFIQI TGLGGSALVG RDLSFKLMKI GYRVACEADT HVQATVSQAL
     KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLAD SPLRRLAHFT LDTVSGETEW
     RSSSMSTRTA QNSVTDLLFV GLVQHQ