RNG_ECO57
ID RNG_ECO57 Reviewed; 489 AA.
AC P0A9J2; P25537; P76677;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ribonuclease G;
DE Short=RNase G;
DE EC=3.1.26.-;
GN Name=rng; Synonyms=cafA; OrderedLocusNames=Z4605, ECs4119;
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).
CC -!- FUNCTION: An endonuclease that acts in the processing of the 5'-end of
CC 16S rRNA and 23S rRNA. It prefers 5'-monophosphorylated substrates and
CC cleaves single-stranded sites rich in A and U residues; contributes to
CC tRNA processing and mRNA turnover. {ECO:0000250|UniProtKB:P0A9J0}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P21513};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513};
CC -!- SUBUNIT: Homodimer, in equilibrium with possible higher multimers.
CC {ECO:0000250|UniProtKB:P0A9J0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J0}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58374.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58374.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB37542.1; -; Genomic_DNA.
DR PIR; G91143; G91143.
DR RefSeq; NP_312146.1; NC_002695.1.
DR RefSeq; WP_000123197.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A9J2; -.
DR SMR; P0A9J2; -.
DR STRING; 155864.EDL933_4468; -.
DR PRIDE; P0A9J2; -.
DR EnsemblBacteria; AAG58374; AAG58374; Z4605.
DR EnsemblBacteria; BAB37542; BAB37542; ECs_4119.
DR GeneID; 67415922; -.
DR GeneID; 916034; -.
DR KEGG; ece:Z4605; -.
DR KEGG; ecs:ECs_4119; -.
DR PATRIC; fig|386585.9.peg.4300; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_6; -.
DR OMA; TKGPRIS; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR004659; RNase_E/G.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR30001; PTHR30001; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00757; RNaseEG; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; rRNA processing; rRNA-binding;
KW tRNA processing; tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0A9J0"
FT CHAIN 2..489
FT /note="Ribonuclease G"
FT /id="PRO_0000097381"
FT DOMAIN 39..128
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513"
SQ SEQUENCE 489 AA; 55364 MW; 9517B3367C455C99 CRC64;
MTAELLVNVT PSETRVAYID GGILQEIHIE REARRGIVGN IYKGRVSRVL PGMQAAFVDI
GLDKAAFLHA SDIMPHTECV AGEEQKQFTV RDISELVRQG QDLMVQVVKD PLGTKGARLT
TDITLPSRYL VFMPGASHVG VSQRIESESE RERLKKVVAE YCDEQGGFII RTAAEGVGEA
ELASDAAYLK RVWTKVMERK KRPQTRYQLY GELALAQRVL RDFADAELDR IRVDSRLTYE
ALLEFTSEYI PEMTSKLEHY TGRQPIFDLF DVENEIQRAL ERKVELKSGG YLIIDQTEAM
TTVDINTGAF VGHRNLDDTI FNTNIEATQA IARQLRLRNL GGIIIIDFID MNNEDHRRRV
LHSLEQALSK DRVKTSVNGF SALGLVEMTR KRTRESIEHV LCNECPTCHG RGTVKTVETV
CYEIMREIVR VHHAYDSDRF LVYASPAVAE ALKGEESHSL AEVEIFVGKQ VKVQIEPLYN
QEQFDVVMM
