MURR_ECOLI
ID MURR_ECOLI Reviewed; 285 AA.
AC P77245;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=HTH-type transcriptional regulator MurR;
DE AltName: Full=MurPQ operon repressor;
GN Name=murR; Synonyms=yfeT; OrderedLocusNames=b2427, JW2420;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A TRANSCRIPTIONAL REGULATOR, PATHWAY, INDUCER, INDUCTION,
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18723630; DOI=10.1128/jb.00642-08;
RA Jaeger T., Mayer C.;
RT "The transcriptional factors MurR and catabolite activator protein regulate
RT N-acetylmuramic acid catabolism in Escherichia coli.";
RL J. Bacteriol. 190:6598-6608(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. Also represses its own transcription.
CC {ECO:0000269|PubMed:18723630}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation
CC [regulation]. {ECO:0000269|PubMed:18723630}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:18723630}.
CC -!- INDUCTION: Repressed by itself and by the cAMP receptor protein crp.
CC {ECO:0000269|PubMed:18723630}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an abolition of the
CC extensive lag phase observed when grown on MurNAc and a 20-fold
CC enhancement of murQ transcription. {ECO:0000269|PubMed:18723630}.
CC -!- MISCELLANEOUS: Neither GlcNAc-6-P, GlcNAc, anhydroMurNAc, MurNAc, nor
CC muramyl dipeptide have an effect on MurR binding to the operator site.
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DR EMBL; U00096; AAC75480.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16310.1; -; Genomic_DNA.
DR PIR; B65017; B65017.
DR RefSeq; NP_416922.1; NC_000913.3.
DR RefSeq; WP_000966470.1; NZ_LN832404.1.
DR AlphaFoldDB; P77245; -.
DR SMR; P77245; -.
DR BioGRID; 4263047; 28.
DR DIP; DIP-12018N; -.
DR IntAct; P77245; 12.
DR STRING; 511145.b2427; -.
DR PaxDb; P77245; -.
DR PRIDE; P77245; -.
DR EnsemblBacteria; AAC75480; AAC75480; b2427.
DR EnsemblBacteria; BAA16310; BAA16310; BAA16310.
DR GeneID; 946568; -.
DR KEGG; ecj:JW2420; -.
DR KEGG; eco:b2427; -.
DR PATRIC; fig|1411691.4.peg.4304; -.
DR EchoBASE; EB3913; -.
DR eggNOG; COG1737; Bacteria.
DR HOGENOM; CLU_055769_0_2_6; -.
DR InParanoid; P77245; -.
DR OMA; DHRIGSM; -.
DR PhylomeDB; P77245; -.
DR BioCyc; EcoCyc:G7262-MON; -.
DR UniPathway; UPA00342; -.
DR PRO; PR:P77245; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IDA:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0043470; P:regulation of carbohydrate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..285
FT /note="HTH-type transcriptional regulator MurR"
FT /id="PRO_0000068625"
FT DOMAIN 1..77
FT /note="HTH rpiR-type"
FT DOMAIN 128..268
FT /note="SIS"
FT DNA_BIND 37..56
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
SQ SEQUENCE 285 AA; 31192 MW; 4235E45DB8B7C3A8 CRC64;
MLYLTKISNA GSEFTENEQK IADFLQANVS ELQSVSSRQM AKQLGISQSS IVKFAQKLGA
QGFTELRMAL IGEYSASREK TNATALHLHS SITSDDSLEV IARKLNREKE LALEQTCALL
DYARLQKIIE VISKAPFIQI TGLGGSALVG RDLSFKLMKI GYRVACEADT HVQATVSQAL
KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLTD SPLRRLAHFT LDTVSGETEW
RSSSMSTRTA QNSVTDLLFV GLVQLNDVES LKMIQRSSEL TQRLK
