RNC_ECO57
ID RNC_ECO57 Reviewed; 226 AA.
AC P0A7Y2; P05797; P06141;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104};
DE Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104};
GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104};
GN OrderedLocusNames=Z3848, ECs3433;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP FUNCTION IN TYPE I TOXIN-ANTITOXIN REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=24203704; DOI=10.1093/nar/gkt1018;
RA Wen J., Won D., Fozo E.M.;
RT "The ZorO-OrzO type I toxin-antitoxin locus: repression by the OrzO
RT antitoxin.";
RL Nucleic Acids Res. 42:1930-1946(2014).
CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC primary rRNA transcript to yield the immediate precursors to the large
CC and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when
CC they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA
CC of type II CRISPR loci if present in the organism (By similarity).
CC Involved in degradation of type I toxin-antitoxin system duplex RNAs
CC (PubMed:24203704). {ECO:0000255|HAMAP-Rule:MF_00104,
CC ECO:0000269|PubMed:24203704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}.
CC -!- DISRUPTION PHENOTYPE: Decreased levels of type I toxin-antitoxin sRNA
CC orzO, and increased toxicity of toxin ZorO.
CC {ECO:0000269|PubMed:24203704}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000255|HAMAP-
CC Rule:MF_00104}.
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DR EMBL; AE005174; AAG57682.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36856.1; -; Genomic_DNA.
DR PIR; A91058; A91058.
DR PIR; F85902; F85902.
DR RefSeq; NP_311460.1; NC_002695.1.
DR RefSeq; WP_001068343.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A7Y2; -.
DR SMR; P0A7Y2; -.
DR STRING; 155864.EDL933_3732; -.
DR EnsemblBacteria; AAG57682; AAG57682; Z3848.
DR EnsemblBacteria; BAB36856; BAB36856; ECs_3433.
DR GeneID; 67416946; -.
DR GeneID; 914894; -.
DR KEGG; ece:Z3848; -.
DR KEGG; ecs:ECs_3433; -.
DR PATRIC; fig|386585.9.peg.3587; -.
DR eggNOG; COG0571; Bacteria.
DR HOGENOM; CLU_000907_1_1_6; -.
DR OMA; LTHKSCK; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; -; 1.
DR HAMAP; MF_00104; RNase_III; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF14622; Ribonucleas_3_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
DR TIGRFAMs; TIGR02191; RNaseIII; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Nuclease; Reference proteome; RNA-binding;
KW rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1..226
FT /note="Ribonuclease 3"
FT /id="PRO_0000180396"
FT DOMAIN 6..128
FT /note="RNase III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT DOMAIN 155..225
FT /note="DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 45
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ SEQUENCE 226 AA; 25550 MW; D9E2858F2E0AA3A5 CRC64;
MNPIVINRLQ RKLGYTFNHQ ELLQQALTHR SASSKHNERL EFLGDSILSY VIANALYHRF
PRVDEGDMSR MRATLVRGNT LAELAREFEL GECLRLGPGE LKSGGFRRES ILADTVEALI
GGVFLDSDIQ TVEKLILNWY QTRLDEISPG DKQKDPKTRL QEYLQGRHLP LPTYLVVQVR
GEAHDQEFTI HCQVSGLSEP VVGTGSSRRK AEQAAAEQAL KKLELE
