ECOLI:RNE

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	rne (ECO:0000255 with HAMAP-Rule:MF_00970) (synonyms: ams, hmp1)
Protein Name(s)	Ribonuclease E (ECO:0000255 with HAMAP-Rule:MF_00970) RNase E (ECO:0000255 with HAMAP-Rule:MF_00970)
External Links
UniProt	P21513
EMBL	U00096 AP009048 X67470 M62747 X54309 L23942
PIR	A64852
RefSeq	NP_415602.1 YP_489352.1
PDB	1SLJ 1SMX 1SN8 2BX2 2C0B 2C4R 2FYM 2VMK 2VRT 3GCM 3GME 3H1C 3H8A
PDBsum	1SLJ 1SMX 1SN8 2BX2 2C0B 2C4R 2FYM 2VMK 2VRT 3GCM 3GME 3H1C 3H8A
DisProt	DP00207
ProteinModelPortal	P21513
SMR	P21513
DIP	DIP-10727N
IntAct	P21513
MINT	MINT-1220086
STRING	511145.b1084
PaxDb	P21513
PRIDE	P21513
EnsemblBacteria	AAC74168 BAA35893
GeneID	12932029 945641
KEGG	ecj:Y75_p1054 eco:b1084
PATRIC	32117409
EchoBASE	EB0852
EcoGene	EG10859
eggNOG	COG1530
HOGENOM	HOG000258027
InParanoid	P21513
KO	K08300
OMA	ENTKEVH
OrthoDB	EOG6PCPTH
BioCyc	EcoCyc:EG10859-MONOMER ECOL316407:JW1071-MONOMER MetaCyc:EG10859-MONOMER
EvolutionaryTrace	P21513
PRO	PR:P21513
Proteomes	UP000000318 UP000000625
Genevestigator	P21513
GO	GO:0005737 GO:0009898 GO:0004521 GO:0000287 GO:0008995 GO:0003723 GO:0008270 GO:0006402 GO:0006401 GO:0000967 GO:0006364 GO:0008033
Gene3D	2.40.50.140
HAMAP	MF_00970
InterPro	IPR012340 IPR021968 IPR003029 IPR019307 IPR028878 IPR004659 IPR022967
Pfam	PF12111 PF10150 PF00575
SMART	SM00316
SUPFAM	SSF50249
TIGRFAMs	TIGR00757
PROSITE	PS50126

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0004519	endonuclease activity	PMID:9790196^[1]	ECO:0000314			F	Two forms of RNA were used, linear and circular. The circular RNA did not have a 5' end and thus could not be digested by RNase E as shown in Figure 2a. The circular RNA was then digested by RNase H and thus linearized as shown in Figure 2b. The now linearized RNA was then digested by RNase E which since the RNA was linear could be digested by RNase E as shown in Figure 2d and Figure 2e. The bands shown in Figures 2d,e are consistent with the digestion sites of both RNase H and RNase E.	complete
enables	GO:0017151	DEAD/H-box RNA helicase binding	PMID:15236960^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A8J8	F	Seeded From UniProt	complete
involved_in	GO:1902280	regulation of ATP-dependent RNA helicase activity	PMID:15236960^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:15236960^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008312	7S RNA binding	PMID:15236960^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006364	rRNA processing	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG11299 PANTHER:PTN001246338	P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18682225^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21513	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15236960^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21513	F	Seeded From UniProt	complete
involved_in	GO:0051289	protein homotetramerization	PMID:14636052^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21513	P	Seeded From UniProt	complete
enables	GO:0008995	ribonuclease E activity	PMID:12417756^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0008033	tRNA processing	PMID:11871663^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006402	mRNA catabolic process	PMID:1846032^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006401	RNA catabolic process	PMID:8415644^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0000967	rRNA 5'-end processing	PMID:10329633^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:25404697^[11]	ECO:0000315	mutant phenotype 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:0004519	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:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0008995	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:0008995	P	Seeded From UniProt	complete
involved_in	GO:0090502	RNA phosphodiester bond hydrolysis, endonucleolytic	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004521	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	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:IPR004659 InterPro:IPR019307	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:IPR004659	F	Seeded From UniProt	complete
involved_in	GO:0006396	RNA processing	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004659 InterPro:IPR028878	P	Seeded From UniProt	complete
enables	GO:0008995	ribonuclease E activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR028878	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:UR000112759	C	Seeded From UniProt	complete
enables	GO:0004521	endoribonuclease activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000112759	F	Seeded From UniProt	complete
involved_in	GO:0006402	mRNA catabolic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000112759	P	Seeded From UniProt	complete
part_of	GO:0009898	cytoplasmic side of plasma membrane	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000112759	C	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000112759	F	Seeded From UniProt	complete
involved_in	GO:0006364	rRNA processing	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000112759	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:UR000112759	F	Seeded From UniProt	complete
involved_in	GO:0008033	tRNA processing	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000112759	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000112759	F	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-KW:KW-0997 UniProtKB-SubCell:SL-0037	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
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0255	F	Seeded From UniProt	complete
involved_in	GO:0006364	rRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0698	P	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
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
involved_in	GO:0008033	tRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0819	P	Seeded From UniProt	complete
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Notes

References

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

↑ Mackie, GA (1998) Ribonuclease E is a 5'-end-dependent endonuclease. Nature 395 720-3 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Callaghan, AJ et al. (2004) Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J. Mol. Biol. 340 965-79 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
↑ Koslover, DJ et al. (2008) The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. Structure 16 1238-44 PubMed GONUTS page
↑ Callaghan, AJ et al. (2003) Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain. Biochemistry 42 13848-55 PubMed GONUTS page
↑ Feng, Y et al. (2002) The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection. Proc. Natl. Acad. Sci. U.S.A. 99 14746-51 PubMed GONUTS page
↑ Li, Z & Deutscher, MP (2002) RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors. RNA 8 97-109 PubMed GONUTS page
↑ Babitzke, P & Kushner, SR (1991) The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 88 1-5 PubMed GONUTS page
↑ Cormack, RS et al. (1993) RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product. Proc. Natl. Acad. Sci. U.S.A. 90 9006-10 PubMed GONUTS page
↑ Li, Z et al. (1999) RNase G (CafA protein) and RNase E are both required for the 5' maturation of 16S ribosomal RNA. EMBO J. 18 2878-85 PubMed GONUTS page
↑ Thompson, KJ et al. (2015) Altering the divalent metal ion preference of RNase E. J. Bacteriol. 197 477-82 PubMed GONUTS page

[PMID:9790196-1] Mackie, GA (1998) Ribonuclease E is a 5'-end-dependent endonuclease. Nature 395 720-3 PubMed GONUTS page

[PMID:15236960-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Callaghan, AJ et al. (2004) Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J. Mol. Biol. 340 965-79 PubMed GONUTS page

[PMID:21873635-3] 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:18682225-4] Koslover, DJ et al. (2008) The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. Structure 16 1238-44 PubMed GONUTS page

[PMID:14636052-5] Callaghan, AJ et al. (2003) Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain. Biochemistry 42 13848-55 PubMed GONUTS page

[PMID:12417756-6] Feng, Y et al. (2002) The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection. Proc. Natl. Acad. Sci. U.S.A. 99 14746-51 PubMed GONUTS page

[PMID:11871663-7] Li, Z & Deutscher, MP (2002) RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors. RNA 8 97-109 PubMed GONUTS page

[PMID:1846032-8] Babitzke, P & Kushner, SR (1991) The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 88 1-5 PubMed GONUTS page

[PMID:8415644-9] Cormack, RS et al. (1993) RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product. Proc. Natl. Acad. Sci. U.S.A. 90 9006-10 PubMed GONUTS page

[PMID:10329633-10] Li, Z et al. (1999) RNase G (CafA protein) and RNase E are both required for the 5' maturation of 16S ribosomal RNA. EMBO J. 18 2878-85 PubMed GONUTS page

[PMID:25404697-11] Thompson, KJ et al. (2015) Altering the divalent metal ion preference of RNase E. J. Bacteriol. 197 477-82 PubMed GONUTS page

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ECOLI:RNE

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References

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