UniProtKB - P0A9J0 (RNG_ECOLI)
Protein
Ribonuclease G
Gene
rng
Organism
Escherichia coli (strain K12)
Status
Functioni
An endonuclease that acts in the processing of the 5'-end of precursors of 16S rRNA (PubMed:10329633, PubMed:10362534, PubMed:10722715, PubMed:20176963, PubMed:24489121, PubMed:26694614). It prefers 5'-monophosphorylated over 5'-OH or 5'-triphosphorylated substrates and cleaves single-stranded sites rich in A and U residues; contributes to RNA turnover (PubMed:10722715, PubMed:11380618, PubMed:12450135, PubMed:18078441, PubMed:21717341, PubMed:10762247). 5'-monophosphate-assisted cleavage requires at least 2 and preferably 3 or more unpaired 5'-terminal nucleotides for cleavage. The optimal spacing between the 5' end and the scissile phosphate appears to be 6 nucleotides. Any sequence of unpaired nucleotides at the 5'-end is tolerated (PubMed:26694614). Processes the 5'-end precursors of 23S rRNA (PubMed:21717341). Participates in processing of tRNA(Pro) (proK and proM) (PubMed:27288443). Also involved in metabolism of some mRNAs (PubMed:11380618, PubMed:12450135, PubMed:18078441). Cells overproducing this protein form chains of cell with cytoplasmic axial filaments (PubMed:8300545). Could be involved in chromosome segregation and cell division. It may be one of the components of the cytoplasmic axial filaments bundles, or merely regulate the formation of this structure (Probable).1 Publication13 Publications
Confers adaptive resistance to aminoglycoside antibiotics through modulation of 16S rRNA processing.1 Publication
Cofactori
Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
Activity regulationi
The presence of a 5'-monophosphate on substrate RNA accelerates its cleavage by catalytically activating the enzyme (PubMed:15197283). In contrast, another group has shown that the enzyme has a higher affinity for 5'-monophosphorylated substrate, which enhances substrate binding in vitro and the decay of RNA in vivo (PubMed:18078441).2 Publications
Kineticsi
kcat is 2.1 min(-1) for 14-base 5'-PO4 substrate and 0.096 min(-1) for 5-OH substrate (PubMed:15197283). kcat is 3.0 min(-1) for 13-base 5'-PO4 substrate and 1.2 min(-1) for 5-OH substrate (PubMed:18078441).2 Publications
- KM=0.23 µM for 5'-phosphorylated 14 base fluorogenic substrate1 Publication
- KM=0.33 µM for 5'-OH 14 base fluorogenic substrate1 Publication
- KM=0.12 µM for 5'-phosphorylated 13 base fluorogenic substrate1 Publication
- KM=21 µM for 5'-OH 13 base fluorogenic substrate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 304 | Magnesium; catalyticBy similarity1 Publication | 1 | |
Metal bindingi | 347 | Magnesium; catalyticBy similarity1 Publication | 1 |
GO - Molecular functioni
- endonuclease activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- ribonuclease activity Source: GO_Central
- ribonuclease G activity Source: EcoCyc
- rRNA binding Source: UniProtKB-KW
- tRNA binding Source: UniProtKB-KW
GO - Biological processi
- cell cycle Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- rRNA processing Source: EcoliWiki
- tRNA processing Source: UniProtKB-KW
Keywordsi
Molecular function | Endonuclease, Hydrolase, Nuclease, RNA-binding, rRNA-binding, tRNA-binding |
Biological process | Cell cycle, Cell division, rRNA processing, tRNA processing |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11299-MONOMER MetaCyc:EG11299-MONOMER |
BRENDAi | 3.1.26.3, 2165 |
Names & Taxonomyi
Protein namesi | Recommended name: Ribonuclease G2 Publications (EC:3.1.26.-)Short name: RNase G2 Publications Alternative name(s): Cytoplasmic axial filament protein1 Publication |
Gene namesi | Name:rng2 Publications Synonyms:cafA1 Publication, orfF1 Publication, yhdF Ordered Locus Names:b3247, JW3216 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm 1 Publication1 Publication
- Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication
- cytoskeleton 1 Publication Note: Possible cytoskeletal location is upon overproduction.1 Publication
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
- cytoskeleton Source: UniProtKB-SubCell
- plasma membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, Cytoplasm, Cytoskeleton, MembranePathology & Biotechi
Disruption phenotypei
Slow processing of the 17S rRNA precursor to 16S rRNA, with significant accumulation of a 16.3S rRNA precursor (PubMed:10329633, PubMed:10362534, PubMed:20176963). Ribosomes with the precursor 16S rRNA show decreased translational fidelity and an increased sensitivity to aminoglycoside antibiotics neomycin and paromomycin (PubMed:20176963). In contrast another group, using independently generated rng deletions in 2 different strains, showed decreased sensitivity to aminoglycoside antibiotics kanamycin, neomycin, paromomycin and streptomycin (PubMed:24489121). A double rne-rng mutated strain no longer processes the 17S rRNA precursor (PubMed:10329633, PubMed:10362534). Significant accumulation of AdhE and enolase, greatly increased stability of adhE and eno mRNA (PubMed:11380618, PubMed:12450135). Accumulation of a 23S rRNA precursor (PubMed:21717341).7 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 131 | V → A: 3.9-fold reduced activity on 5'-PO(4) substrate, 1.9-fold reduced activity on 5'-OH substrate. Has wild-type 16S rRNA in vivo. 1 Publication | 1 | |
Mutagenesisi | 171 | R → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 171 | R → K: 34-fold reduced activity on 5'-PO(4) substrate, 2.4-fold reduced activity on 5'-OH substrate. Binds 5'-PO(4) substrate 65-fold less well than wild-type, kcat is nearly wild-type. Has wild-type 16S rRNA in vivo. 1 Publication | 1 | |
Mutagenesisi | 172 | T → V: 82-fold reduced activity on 5'-PO(4) substrate, 4.9-fold reduced activity on 5'-OH substrate. 1 Publication | 1 | |
Mutagenesisi | 304 | D → N: Loss of activity. Accumulates about 50% 16.3S rRNA, 50% wild-type 16SrRNA in vivo. 1 Publication | 1 | |
Mutagenesisi | 347 | D → N: Loss of activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000097383 | 2 – 489 | Ribonuclease GAdd BLAST | 488 |
Proteomic databases
jPOSTi | P0A9J0 |
PaxDbi | P0A9J0 |
PRIDEi | P0A9J0 |
Expressioni
Inductioni
Its mRNA is degraded by RNase III (rnc); in the presence of aminoglycoside antibiotics levels of rng mRNA decrease, leading to longer precursor 16S rRNA in the ribosome, which prevents antibiotic-binding and thus increases resistance to aminoglycosides.1 Publication
Interactioni
Subunit structurei
Homodimer, in equilibrium with possible higher multimers.
3 PublicationsBinary interactionsi
P0A9J0
With | #Exp. | IntAct |
---|---|---|
rpsD [P0A7V8] | 2 | EBI-545964,EBI-543939 |
Protein-protein interaction databases
BioGRIDi | 4262071, 231 interactors 852056, 1 interactor |
DIPi | DIP-48098N |
IntActi | P0A9J0, 20 interactors |
STRINGi | 511145.b3247 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 39 – 128 | S1 motifPROSITE-ProRule annotationAdd BLAST | 90 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 244 – 489 | Required for function, when replaced by GVHSRDDKQAGALHRTPADFRSL in mutant BUMMER, cells accumulate 16.3S rRNA precursor1 PublicationAdd BLAST | 246 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1530, Bacteria |
HOGENOMi | CLU_003468_5_3_6 |
InParanoidi | P0A9J0 |
PhylomeDBi | P0A9J0 |
Family and domain databases
InterProi | View protein in InterPro IPR012340, NA-bd_OB-fold IPR019307, RNA-bd_AU-1/RNase_E/G IPR004659, RNase_E/G IPR022967, S1_dom IPR003029, S1_domain |
Pfami | View protein in Pfam PF10150, RNase_E_G, 1 hit PF00575, S1, 1 hit |
SMARTi | View protein in SMART SM00316, S1, 1 hit |
SUPFAMi | SSF50249, SSF50249, 1 hit |
TIGRFAMsi | TIGR00757, RNaseEG, 1 hit |
PROSITEi | View protein in PROSITE PS50126, S1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A9J0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTAELLVNVT PSETRVAYID GGILQEIHIE REARRGIVGN IYKGRVSRVL
60 70 80 90 100
PGMQAAFVDI GLDKAAFLHA SDIMPHTECV AGEEQKQFTV RDISELVRQG
110 120 130 140 150
QDLMVQVVKD PLGTKGARLT TDITLPSRYL VFMPGASHVG VSQRIESESE
160 170 180 190 200
RERLKKVVAE YCDEQGGFII RTAAEGVGEA ELASDAAYLK RVWTKVMERK
210 220 230 240 250
KRPQTRYQLY GELALAQRVL RDFADAELDR IRVDSRLTYE ALLEFTSEYI
260 270 280 290 300
PEMTSKLEHY TGRQPIFDLF DVENEIQRAL ERKVELKSGG YLIIDQTEAM
310 320 330 340 350
TTVDINTGAF VGHRNLDDTI FNTNIEATQA IARQLRLRNL GGIIIIDFID
360 370 380 390 400
MNNEDHRRRV LHSLEQALSK DRVKTSVNGF SALGLVEMTR KRTRESIEHV
410 420 430 440 450
LCNECPTCHG RGTVKTVETV CYEIMREIVR VHHAYDSDRF LVYASPAVAE
460 470 480
ALKGEESHSL AEVEIFVGKQ VKVQIEPLYN QEQFDVVMM
Sequence cautioni
The sequence AAA58050 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X57166 Genomic DNA Translation: CAA40457.1 U18997 Genomic DNA Translation: AAA58050.1 Different initiation. U00096 Genomic DNA Translation: AAC76279.2 AP009048 Genomic DNA Translation: BAE77289.1 |
PIRi | A65117 |
RefSeqi | NP_417713.2, NC_000913.3 WP_000123197.1, NZ_STEB01000012.1 |
Genome annotation databases
EnsemblBacteriai | AAC76279; AAC76279; b3247 BAE77289; BAE77289; BAE77289 |
GeneIDi | 52075173 947744 |
KEGGi | ecj:JW3216 eco:b3247 |
PATRICi | fig|1411691.4.peg.3482 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X57166 Genomic DNA Translation: CAA40457.1 U18997 Genomic DNA Translation: AAA58050.1 Different initiation. U00096 Genomic DNA Translation: AAC76279.2 AP009048 Genomic DNA Translation: BAE77289.1 |
PIRi | A65117 |
RefSeqi | NP_417713.2, NC_000913.3 WP_000123197.1, NZ_STEB01000012.1 |
3D structure databases
SMRi | P0A9J0 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4262071, 231 interactors 852056, 1 interactor |
DIPi | DIP-48098N |
IntActi | P0A9J0, 20 interactors |
STRINGi | 511145.b3247 |
Proteomic databases
jPOSTi | P0A9J0 |
PaxDbi | P0A9J0 |
PRIDEi | P0A9J0 |
Genome annotation databases
EnsemblBacteriai | AAC76279; AAC76279; b3247 BAE77289; BAE77289; BAE77289 |
GeneIDi | 52075173 947744 |
KEGGi | ecj:JW3216 eco:b3247 |
PATRICi | fig|1411691.4.peg.3482 |
Organism-specific databases
EchoBASEi | EB1276 |
Phylogenomic databases
eggNOGi | COG1530, Bacteria |
HOGENOMi | CLU_003468_5_3_6 |
InParanoidi | P0A9J0 |
PhylomeDBi | P0A9J0 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11299-MONOMER MetaCyc:EG11299-MONOMER |
BRENDAi | 3.1.26.3, 2165 |
Miscellaneous databases
PROi | PR:P0A9J0 |
Family and domain databases
InterProi | View protein in InterPro IPR012340, NA-bd_OB-fold IPR019307, RNA-bd_AU-1/RNase_E/G IPR004659, RNase_E/G IPR022967, S1_dom IPR003029, S1_domain |
Pfami | View protein in Pfam PF10150, RNase_E_G, 1 hit PF00575, S1, 1 hit |
SMARTi | View protein in SMART SM00316, S1, 1 hit |
SUPFAMi | SSF50249, SSF50249, 1 hit |
TIGRFAMsi | TIGR00757, RNaseEG, 1 hit |
PROSITEi | View protein in PROSITE PS50126, S1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RNG_ECOLI | |
Accessioni | P0A9J0Primary (citable) accession number: P0A9J0 Secondary accession number(s): P25537, P76677, Q2M8W7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 19, 2005 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 122 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families