ID MURR_ECOSM Reviewed; 285 AA.
AC B1LMM1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, 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};
GN OrderedLocusNames=EcSMS35_2582;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB19433.1; -; Genomic_DNA.
DR RefSeq; WP_000966459.1; NC_010498.1.
DR AlphaFoldDB; B1LMM1; -.
DR SMR; B1LMM1; -.
DR KEGG; ecm:EcSMS35_2582; -.
DR HOGENOM; CLU_055769_0_2_6; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000007011; 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 DNA-templated transcription; 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; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_02108; HTH_type_MurR; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR000281; HTH_RpiR.
DR InterPro; IPR047640; RpiR-like.
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 PANTHER; PTHR30514; GLUCOKINASE; 1.
DR PANTHER; PTHR30514:SF17; HTH-TYPE TRANSCRIPTIONAL REGULATOR MURR; 1.
DR Pfam; PF01418; HTH_6; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF53697; SIS domain; 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_0000387760"
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; 31355 MW; E7E9A3BE75976C69 CRC64;
MLYLTKIRNA ESEFTGNEQK IADFLRANVS ELKSVSSRKM AKQLGISQSS IVKFAQKLGA
QGFTELRMAL IGEYSASREK TNATALHLHS SITSDDSLEV IARKLNREKE QALEQTCALF
DYARLQKIIE VISKAPFIQI TGLGGSALVG RDLSFKLMKI GYRVACEADT HVQATVSQAL
KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLTD SPLRRLAHYT LDTVSGETEW
RSSSMSTRTA QNSVTDLLFV GLVQLNDVES LKMIERSSEL TQRLK
//
