Standard name	Rng
Synonyms	ribonuclease G^[1], B3247^[2]^[1], AdhR^[2]^[1], Rng^[2]^[1], YhdF^[2]^[1], CafA^[2]^[1]
Product description	ribonuclease G (RNAse G)^[2]^[3]; Component of ; ribonuclease G (RNAse G)^[3]
EC number (for enzymes)	3.1.4^[1]
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Notes

Function

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Gene Ontology
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Qualifier	GO ID	GO term name	Reference(s)	Evidence Code	with/from	Aspect	Notes	Status
	GO:0008996	ribonuclease G activity	PMID:10722715^[4]	IDA: Inferred from Direct Assay		F	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0006364	rRNA processing	PMID:10362534^[6]	IMP: Inferred from Mutant Phenotype		P	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0051301	cell division	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0132	P	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0016787	hydrolase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0378	F	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0007049	cell cycle	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0131	P	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0006396	RNA processing	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR004659	P	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0005856	cytoskeleton	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0206	C	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0005737	cytoplasm	GO_REF:0000002 GO_REF:0000004	IEA: Inferred from Electronic Annotation	InterPro:IPR004659 SP_KW:KW-0963	C	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0004540	ribonuclease activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR004659	F	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0004519	endonuclease activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0255	F	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0004518	nuclease activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0540	F	Seeded from EcoCyc 12.5 ^[5]	complete
	GO:0003723	RNA binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003029	F	Seeded from EcoCyc 12.5 ^[5]	complete
NOT	GO:0009451	RNA modification				P	Seeded from EcoCyc 11.1^[3]. I think this annotation is incorrect. RNA modification is The covalent alteration of one or more nucleotides within an RNA molecule to produce an RNA molecule with a sequence that differs from that coded genetically." Rng processes 16S RNA, but I could find no evidence that it modifies the sequence.	required field missing
	GO:0006401	RNA catabolic process				P	Seeded from EcoCyc 11.1^[3]. I think this annotation is incorrect because processing by Rng is involved in the synthesis of functional ribosomes not the turnover of ribosomes (DAS, TAMU).	required field missing
NOT	GO:0000910	cytokinesis				P	Seeded from EcoCyc 11.1^[3]. Overproduction of CafA causes a cell division defect: chains of cells and minicells form when expression of cafA from a multicopy plasmid is induced by the addition of IPTG ^[7]/>. Long axial filaments were also observed to form. (DAS, TAMU)	required field missing
	GO:0008996	ribonuclease G activity	PMID:10722715^[4]	IDA: Inferred from Direct Assay		F		complete
	GO:0006364	rRNA processing	PMID:10362534^[6]	IMP: Inferred from Mutant Phenotype		P		complete
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Interactions

Partner Type	Partner	Notes	References
Protein	Subunits of ribonuclease G (RNAse G)	could be indirect
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Notes

Localization

Compartment	Description	Evidence	Notes
cytoplasm			From EcoCyc^[3]
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Notes

Structure and Physical Properties

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Physical Properties

Sequence	at EcoCyc MRKGINMTAE LLVNVTPSET RVAYIDGGIL QEIHIEREAR RGIVGNIYKG RVSRVLPGMQ AAFVDIGLDK AAFLHASDIM PHTECVAGEE QKQFTVRDIS ELVRQGQDLM VQVVKDPLGT KGARLTTDIT LPSRYLVFMP GASHVGVSQR IESESERERL KKVVAEYCDE QGGFIIRTAA EGVGEAELAS DAAYLKRVWT KVMERKKRPQ TRYQLYGELA LAQRVLRDFA DAELDRIRVD SRLTYEALLE FTSEYIPEMT SKLEHYTGRQ PIFDLFDVEN EIQRALERKV ELKSGGYLII DQTEAMTTVD INTGAFVGHR NLDDTIFNTN IEATQAIARQ LRLRNLGGII IIDFIDMNNE DHRRRVLHSL EQALSKDRVK TSVNGFSALG LVEMTRKRTR ESIEHVLCNE CPTCHGRGTV KTVETVCYEI MREIVRVHHA YDSDRFLVYA SPAVAEALKG EESHSLAEVE IFVGKQVKVQ IEPLYNQEQF DVVMM
Mol. Wt	55.36 kDa (calc) ^[2]
pI
Extinction coefficient	27850 - 28600 (calc based on 15 Y, 1 W, and 6 C residues)
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Domains/Motifs/Modification Sites

Type	Residues	Description	Notes
Domain	39 - 128	S1 motif	UniProt:P0A9J0
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Structure

Structures	No results found.
Models	View models at: EcoliPredict ModBase PSI-PRED Protein Quaternary Structure (PQS) Genomes TO Protein (GTOP)
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Structures

No results found.

Models

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Notes

Gene Product Resources

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Resource type	Source	Notes/Reference
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Notes

Accessions in Other Databases

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Database	Accession	Notes
EcoCyc (EcoliWiki Page)	EcoCyc:EG11299-MONOMER
UniProt (EcoliWiki Page)	UniProt:P0A9J0
PFAM (EcoliWiki Page)	PFAM:PF00575
RefSeq (EcoliWiki Page)	RefSeq:NP_417713
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Notes

Links

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Name	URL	Comments
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References

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↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
↑ ^4.0 ^4.1 Tock MR et al. (2000) The CafA protein required for the 5'-maturation of 16 S rRNA is a 5'-end-dependent ribonuclease that has context-dependent broad sequence specificity. J Biol Chem 275: 8726-32 PubMed EcoliWiki page
↑ ^5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
↑ ^6.0 ^6.1 Wachi M et al. (1999) Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5' end of 16S rRNA. Biochem Biophys Res Commun 259: 483-8 PubMed EcoliWiki page
↑ Okada Y et al. (1994) Cytoplasmic axial filaments in Escherichia coli cells: possible function in the mechanism of chromosome segregation and cell division. J Bacteriol 176: 917-22 PubMed EcoliWiki page

rng:Gene Product(s)

From EcoliWiki

Nomenclature

Notes

Function

Notes

Localization

Notes

Structure and Physical Properties

Notes

Gene Product Resources

Notes

Accessions in Other Databases

Notes

Links

References

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