ECOLI:RNR

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	rnr (synonyms: vacB, yjeC)
Protein Name(s)	Ribonuclease R RNase R Protein VacB
External Links
UniProt	P21499
EMBL	U14003 U00096 AP009048 J04199
PIR	S56404
RefSeq	NP_418600.4 YP_492321.1
ProteinModelPortal	P21499
SMR	P21499
DIP	DIP-10733N
IntAct	P21499
STRING	511145.b4179
PaxDb	P21499
PRIDE	P21499
EnsemblBacteria	AAC77136 BAE78180
GeneID	12932898 948692
KEGG	ecj:Y75_p4065 eco:b4179
PATRIC	32123931
EchoBASE	EB1239
EcoGene	EG11259
eggNOG	COG0557
HOGENOM	HOG000071120
InParanoid	P21499
KO	K12573
OMA	GFFVRLN
OrthoDB	EOG6Q5NRD
PhylomeDB	P21499
BioCyc	EcoCyc:EG11259-MONOMER ECOL316407:JW5741-MONOMER MetaCyc:EG11259-MONOMER RETL1328306-WGS:GSTH-1661-MONOMER
PRO	PR:P21499
Proteomes	UP000000318 UP000000625
Genevestigator	P21499
GO	GO:0005737 GO:0034458 GO:0000175 GO:0016896 GO:0008859 GO:0004540 GO:0008997 GO:0003723 GO:0006402 GO:0034470 GO:0009405 GO:0009409 GO:0090501 GO:0090503
Gene3D	2.40.50.140
HAMAP	MF_01895
InterPro	IPR011129 IPR012340 IPR003029 IPR013223 IPR022966 IPR004476 IPR011805 IPR013668 IPR022967
Pfam	PF08461 PF08206 PF00575
SMART	SM00357 SM00316
SUPFAM	SSF50249
TIGRFAMs	TIGR00358 TIGR02063
PROSITE	PS01175 PS50126

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0016787	hydrolase activity	PMID:9603904^[1] ECOCYC:EG11259	ECO:0000315			F	Table 3 illustrates the necessity of Rnr as Rnr- mutants did not grow on the plates as wild type and Rnr- mutants that still contained other functional Rnases grew.	complete
part_of	GO:0005829	cytosol	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11259 EcoGene:EG11620 PANTHER:PTN000599356	C	Seeded From UniProt	complete
enables	GO:0016896	exoribonuclease activity, producing 5'-phosphomonoesters	PMID:11948193^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008997	ribonuclease R activity	PMID:11948193^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004540	ribonuclease activity	PMID:9603904^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0034470	ncRNA processing	PMID:14622421^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0034458	3'-5' RNA helicase activity	PMID:20023028^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009409	response to cold	PMID:14622421^[4]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008997	ribonuclease R activity	PMID:11948193^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006402	mRNA catabolic process	PMID:15664199^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0000175	3'-5'-exoribonuclease activity	PMID:336626^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000175	3'-5'-exoribonuclease activity	PMID:11948193^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004518	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004527	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004518	P	Seeded From UniProt	complete
involved_in	GO:0090501	RNA phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004540	P	Seeded From UniProt	complete
involved_in	GO:0090501	RNA phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008997	P	Seeded From UniProt	complete
involved_in	GO:0090501	RNA phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008997	P	Seeded From UniProt	complete
involved_in	GO:0090501	RNA phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004540	P	Seeded From UniProt	complete
involved_in	GO:0090503	RNA phosphodiester bond hydrolysis, exonucleolytic	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0008859	P	Seeded From UniProt	complete
involved_in	GO:0090503	RNA phosphodiester bond hydrolysis, exonucleolytic	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0000175	P	Seeded From UniProt	complete
involved_in	GO:0090503	RNA phosphodiester bond hydrolysis, exonucleolytic	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0016896	P	Seeded From UniProt	complete
involved_in	GO:0090503	RNA phosphodiester bond hydrolysis, exonucleolytic	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0000175	P	Seeded From UniProt	complete
involved_in	GO:0090503	RNA phosphodiester bond hydrolysis, exonucleolytic	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0008859	P	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003029 InterPro:IPR011129	F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001900 InterPro:IPR004476 InterPro:IPR011805	F	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011805	F	Seeded From UniProt	complete
enables	GO:0004540	ribonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001900 InterPro:IPR004476	F	Seeded From UniProt	complete
involved_in	GO:0016070	RNA metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004476	P	Seeded From UniProt	complete
enables	GO:0008859	exoribonuclease II activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.13.1	F	Seeded From UniProt	complete
involved_in	GO:0016070	RNA metabolic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000056594	P	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000056594	F	Seeded From UniProt	complete
enables	GO:0008859	exoribonuclease II activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000056594	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000056594	C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F	Seeded From UniProt	complete
enables	GO:0004518	nuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0540	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0009405	pathogenesis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0843	P	Seeded From UniProt	complete
enables	GO:0004527	exonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0269	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Cheng, ZF et al. (1998) The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R. J. Biol. Chem. 273 14077-80 PubMed GONUTS page
↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Cheng, ZF & Deutscher, MP (2002) Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J. Biol. Chem. 277 21624-9 PubMed GONUTS page
↑ ^4.0 ^4.1 Cairrão, F et al. (2003) Cold shock induction of RNase R and its role in the maturation of the quality control mediator SsrA/tmRNA. Mol. Microbiol. 50 1349-60 PubMed GONUTS page
↑ Awano, N et al. (2010) Escherichia coli RNase R has dual activities, helicase and RNase. J. Bacteriol. 192 1344-52 PubMed GONUTS page
↑ Cheng, ZF & Deutscher, MP (2005) An important role for RNase R in mRNA decay. Mol. Cell 17 313-8 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Kasai, T et al. (1977) Exoribonucleases in wild type Escherichia coli and RNase II-deficient mutants. J. Biol. Chem. 252 8950-6 PubMed GONUTS page

[PMID:9603904-1] 1.0 ^1.1 Cheng, ZF et al. (1998) The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R. J. Biol. Chem. 273 14077-80 PubMed GONUTS page

[PMID:21873635-2] Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:11948193-3] 3.0 ^3.1 ^3.2 ^3.3 Cheng, ZF & Deutscher, MP (2002) Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J. Biol. Chem. 277 21624-9 PubMed GONUTS page

[PMID:14622421-4] 4.0 ^4.1 Cairrão, F et al. (2003) Cold shock induction of RNase R and its role in the maturation of the quality control mediator SsrA/tmRNA. Mol. Microbiol. 50 1349-60 PubMed GONUTS page

[PMID:20023028-5] Awano, N et al. (2010) Escherichia coli RNase R has dual activities, helicase and RNase. J. Bacteriol. 192 1344-52 PubMed GONUTS page

[PMID:15664199-6] Cheng, ZF & Deutscher, MP (2005) An important role for RNase R in mRNA decay. Mol. Cell 17 313-8 PubMed GONUTS page

[PMID:18304323-7] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:336626-8] Kasai, T et al. (1977) Exoribonucleases in wild type Escherichia coli and RNase II-deficient mutants. J. Biol. Chem. 252 8950-6 PubMed GONUTS page

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ECOLI:RNR

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