MYCTU:RELA

Species (Taxon ID)	Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s)	relA
Protein Name(s)	Bifunctional (p)ppGpp synthase/hydrolase RelA GTP pyrophosphokinase (p)ppGpp synthase ATP:GTP 3'-pyrophosphotransferase Stringent response-like protein ppGpp synthase II Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase Penta-phosphate guanosine-3'-pyrophosphohydrolase (ppGpp)ase
External Links
UniProt	P9WHG9
EMBL	AL123456
PIR	F70725
RefSeq	NP_217099.1 YP_006516024.1
ProteinModelPortal	P9WHG9
SMR	P9WHG9
GeneID	13319303 887888
KEGG	mtu:Rv2583c mtv:RVBD_2583c
TubercuList	Rv2583c
KO	K00951
UniPathway	UPA00908 UPA00908
Proteomes	UP000001584
GO	GO:0005618 GO:0005886 GO:0016597 GO:0005524 GO:0005525 GO:0008728 GO:0008893 GO:0016301 GO:0030145 GO:0015970 GO:0009405 GO:0015968
Gene3D	3.10.20.30
InterPro	IPR002912 IPR012675 IPR003607 IPR004811 IPR007685 IPR004095 IPR012676
Pfam	PF04607 PF02824
SMART	SM00471 SM00954
SUPFAM	SSF81271
TIGRFAMs	TIGR00691
PROSITE	PS51671

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0005886	plasma membrane	PMID:15525680^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005618	cell wall	PMID:15525680^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0030145	manganese ion binding	PMID:10375643^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0015968	stringent response	PMID:10940033^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009405	pathogenesis	PMID:12897239^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008893	guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity	PMID:10995231^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008893	guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity	PMID:10375643^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008728	GTP diphosphokinase activity	PMID:10375643^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000479633 UniProtKB:P9WHG9	C	Seeded From UniProt	complete
part_of	GO:0005618	cell wall	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000479633 UniProtKB:P9WHG9	C	Seeded From UniProt	complete
involved_in	GO:0015969	guanosine tetraphosphate metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004811 InterPro:IPR007685	P	Seeded From UniProt	complete
enables	GO:0008728	GTP diphosphokinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.6.5	F	Seeded From UniProt	complete
enables	GO:0008893	guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.7.2	F	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:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F	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:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F	Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
involved_in	GO:0015970	guanosine tetraphosphate biosynthetic process	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00908	P	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 Mawuenyega, KG et al. (2005) Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 16 396-404 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Avarbock, D et al. (1999) Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis. Gene 233 261-9 PubMed GONUTS page
↑ Primm, TP et al. (2000) The stringent response of Mycobacterium tuberculosis is required for long-term survival. J. Bacteriol. 182 4889-98 PubMed GONUTS page
↑ Dahl, JL et al. (2003) The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice. Proc. Natl. Acad. Sci. U.S.A. 100 10026-31 PubMed GONUTS page
↑ Avarbock, D et al. (2000) Differential regulation of opposing RelMtb activities by the aminoacylation state of a tRNA.ribosome.mRNA.RelMtb complex. Biochemistry 39 11640-8 PubMed GONUTS page
↑ ^6.0 ^6.1 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:15525680-1] 1.0 ^1.1 Mawuenyega, KG et al. (2005) Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 16 396-404 PubMed GONUTS page

[PMID:10375643-2] 2.0 ^2.1 ^2.2 Avarbock, D et al. (1999) Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis. Gene 233 261-9 PubMed GONUTS page

[PMID:10940033-3] Primm, TP et al. (2000) The stringent response of Mycobacterium tuberculosis is required for long-term survival. J. Bacteriol. 182 4889-98 PubMed GONUTS page

[PMID:12897239-4] Dahl, JL et al. (2003) The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice. Proc. Natl. Acad. Sci. U.S.A. 100 10026-31 PubMed GONUTS page

[PMID:10995231-5] Avarbock, D et al. (2000) Differential regulation of opposing RelMtb activities by the aminoacylation state of a tRNA.ribosome.mRNA.RelMtb complex. Biochemistry 39 11640-8 PubMed GONUTS page

[PMID:21873635-6] 6.0 ^6.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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MYCTU:RELA

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