RNG_SALTS
ID RNG_SALTS Reviewed; 489 AA.
AC A0A0H3NGK0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Ribonuclease G;
DE Short=RNase G;
DE EC=3.1.26.-;
GN Name=rng {ECO:0000303|PubMed:24489121};
GN Synonyms=cafA {ECO:0000303|PubMed:22538806}; OrderedLocusNames=SL1344_3342;
OS Salmonella typhimurium (strain SL1344).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=216597;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL1344;
RX PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT "The transcriptional landscape and small RNAs of Salmonella enterica
RT serovar Typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
RN [2]
RP FUNCTION IN 16S RRNA MATURATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=SL1344;
RX PubMed=24489121; DOI=10.1093/nar/gku093;
RA Song W., Kim Y.H., Sim S.H., Hwang S., Lee J.H., Lee Y., Bae J., Hwang J.,
RA Lee K.;
RT "Antibiotic stress-induced modulation of the endoribonucleolytic activity
RT of RNase III and RNase G confers resistance to aminoglycoside antibiotics
RT in Escherichia coli.";
RL Nucleic Acids Res. 42:4669-4681(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=SL1344;
RX PubMed=30742606; DOI=10.1371/journal.pgen.1007646;
RA Ben-Zvi T., Pushkarev A., Seri H., Elgrably-Weiss M., Papenfort K.,
RA Altuvia S.;
RT "mRNA dynamics and alternative conformations adopted under low and high
RT arginine concentrations control polyamine biosynthesis in Salmonella.";
RL PLoS Genet. 15:e1007646-e1007646(2019).
CC -!- FUNCTION: Acts in the processing of the 5'-end of precursors of 16S
CC rRNA. Confers adaptive resistance to aminoglycoside antibiotics through
CC modulation of 16S rRNA processing (PubMed:24489121). An
CC endoribonuclease, it prefers 5'-monophosphorylated substrates and
CC cleaves single-stranded sites rich in A and U residues; also
CC contributes to 23S rRNA processing, tRNA processing and mRNA turnover
CC (By similarity). Involved in decay of speF mRNA, has a preference for
CC adenine nucleotides (PubMed:30742606). {ECO:0000250|UniProtKB:P0A9J0,
CC ECO:0000269|PubMed:24489121, ECO:0000269|PubMed:30742606}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A9J0};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A9J0};
CC -!- SUBUNIT: Homodimer, and possible higher multimers.
CC {ECO:0000250|UniProtKB:P0A9J0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J0}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in rich media. Significant
CC accumulation of a 16S rRNA precursor. Increased resistance to
CC aminoglycoside antibiotics kanamycin and paramomycin (PubMed:24489121).
CC Increased lifetime of speF mRNA. {ECO:0000269|PubMed:24489121,
CC ECO:0000269|PubMed:30742606}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC {ECO:0000305}.
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DR EMBL; FQ312003; CBW19438.1; -; Genomic_DNA.
DR RefSeq; WP_000123188.1; NZ_QASL01000018.1.
DR AlphaFoldDB; A0A0H3NGK0; -.
DR SMR; A0A0H3NGK0; -.
DR EnsemblBacteria; CBW19438; CBW19438; SL1344_3342.
DR KEGG; sey:SL1344_3342; -.
DR PATRIC; fig|216597.6.peg.3723; -.
DR HOGENOM; CLU_003468_5_3_6; -.
DR OMA; TKGPRIS; -.
DR BioCyc; SENT216597:SL1344_RS17405-MON; -.
DR Proteomes; UP000008962; 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 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW RNA-binding; rRNA processing; rRNA-binding; tRNA processing; tRNA-binding.
FT CHAIN 1..489
FT /note="Ribonuclease G"
FT /id="PRO_0000450348"
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:P0A9J0"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0A9J0"
SQ SEQUENCE 489 AA; 55436 MW; 272D75896425FB5A CRC64;
MTAELLVNVT PSETRVAYID GGILQEIHIE REARRGIVGN IYKGRVSRVL PGMQAAFVDI
GLDKAAFLHA SDIMPHTECV AGDEQKQFTV RDISELVRQG QDLMVQVVKD PLGTKGARLT
TDITLPSRYL VFMPGASHVG VSQRIESESE RERLKKVVAE YCDEQGGFII RTAAEGVCEE
DLASDAAYLK RVWTKVMERK KRPQTRYQMY GELALAQRVL RDFADAQLDR IRVDSRLTYE
SLLEFTAEYI PEMTSKLEHY SGHQPIFDLY DVENEIQRAL ERKVELKSGG YLIIDQTEAM
TTVDINTGAF VGHRNLDDTI FNTNIEATQA IARQLRLRNL GGIIIIDFID MNNEDHRRRV
LHSLEQALSK DRVKTSINGF SPLGLVEMTR KRTRESVEHV LCNECPTCHG RGTVKTVETV
CYEIMREIVR VHHAYDSDRF LVYASPAVAE ALKGEESHAL AEVEIFVGKQ VKVQVEPLYN
QEQFDVVMM
