RNG_ECOL6
ID RNG_ECOL6 Reviewed; 489 AA.
AC P0A9J1; P25537; P76677;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Ribonuclease G;
DE Short=RNase G;
DE EC=3.1.26.-;
GN Name=rng; Synonyms=cafA; OrderedLocusNames=c4001;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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=AAN82441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014075; AAN82441.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000123197.1; NC_004431.1.
DR AlphaFoldDB; P0A9J1; -.
DR SMR; P0A9J1; -.
DR STRING; 199310.c4001; -.
DR EnsemblBacteria; AAN82441; AAN82441; c4001.
DR GeneID; 67415922; -.
DR KEGG; ecc:c4001; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_6; -.
DR OMA; TKGPRIS; -.
DR Proteomes; UP000001410; 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 RNA-binding; rRNA processing; rRNA-binding; 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_0000097382"
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
