RNG_SHIFL
ID RNG_SHIFL Reviewed; 489 AA.
AC P0A9J3; P25537; P76677;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ribonuclease G;
DE Short=RNase G;
DE EC=3.1.26.-;
GN Name=rng; Synonyms=cafA; OrderedLocusNames=SF3285, S3502;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
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DR EMBL; AE005674; AAN44749.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18560.1; -; Genomic_DNA.
DR RefSeq; NP_709042.2; NC_004337.2.
DR RefSeq; WP_000123197.1; NZ_WPGW01000026.1.
DR AlphaFoldDB; P0A9J3; -.
DR SMR; P0A9J3; -.
DR STRING; 198214.SF3285; -.
DR EnsemblBacteria; AAN44749; AAN44749; SF3285.
DR EnsemblBacteria; AAP18560; AAP18560; S3502.
DR GeneID; 1025290; -.
DR GeneID; 67415922; -.
DR KEGG; sfl:SF3285; -.
DR KEGG; sfx:S3502; -.
DR PATRIC; fig|198214.7.peg.3892; -.
DR HOGENOM; CLU_003468_5_3_6; -.
DR OMA; TKGPRIS; -.
DR OrthoDB; 1209444at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000097385"
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
