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MYCTU:RELA

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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 Extension 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

Notes

References

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

  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
  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
  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
  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
  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
  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