MURR_SHISS
ID MURR_SHISS Reviewed; 285 AA.
AC Q3YZB5;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=SSON_2516;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ89147.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YZB5; -.
DR SMR; Q3YZB5; -.
DR EnsemblBacteria; AAZ89147; AAZ89147; SSON_2516.
DR KEGG; ssn:SSON_2516; -.
DR HOGENOM; CLU_055769_0_2_6; -.
DR OMA; DHRIGSM; -.
DR UniPathway; UPA00342; -.
DR Proteomes; UP000002529; 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_0000387776"
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; 31425 MW; EA0FCE323E177E45 CRC64;
MLYLTKIRNA ESEFTENEQK IADFLRANVS ELKSVSSRKM AKQLGISQSS IVKFAQKLGA
QGFTELRMAL IGEYSASREK TNATALHLHS SITSDDSLEV IARKLNREKE LALEQTCALF
DYARLQKIIE VISKAPFIQI TGLGGSALVG RDLSFKLMKI GYRVAYEADT HVQATVSQAL
KKGDVQIAIS YSGSKKEIVL CAEAARKQGA TVIAITSLAD SPLRRLAHFT LDTVSGETEW
RSSSMSTRTA QNSVTDLLFV GLVQLNDVES LKMIQRSSEL TQRLK