MURR_ECO55
ID MURR_ECO55 Reviewed; 285 AA.
AC B7LCH1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=EC55989_2716;
OS Escherichia coli (strain 55989 / EAEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55989 / EAEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928145; CAU98582.1; -; Genomic_DNA.
DR RefSeq; WP_000966471.1; NC_011748.1.
DR AlphaFoldDB; B7LCH1; -.
DR SMR; B7LCH1; -.
DR EnsemblBacteria; CAU98582; CAU98582; EC55989_2716.
DR KEGG; eck:EC55989_2716; -.
DR HOGENOM; CLU_055769_0_2_6; -.
DR OMA; DHRIGSM; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000000746; 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_0000387753"
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; 31212 MW; 2ADBA9029A18BD41 CRC64;
MLYLTKISNA GSEFTENEQK IADFLQANVS ELQSVSSRQM AKQLGISQSS IVKFAQKLGA
QGFTELRMAL IGEYSASREK TNATALHLHS SITSDDSLEV IARKLNREKE LALEQTCSLF
DYARLQKIIE VISKAPFIQI TGLGGSALVG RDLSFKLMKI GYRVACEADT HVQATVSQAL
KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLAD SPLRRLAHFT LDTVSGETEW
RSSSMSTRTA QNSVTDLLFV GLVQLNDVES LKMIQRSSEL TQRLK