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InterPro: IPR007685 RelA/SpoT

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UniProtKB

Matches:

3296 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Architectures
Accession List
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Accession

IPR007685 RelA_SpoT

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF04607	RelA_SpoT	3296
Signatures in BioMart

InterPro Relationships Help

Found in

IPR004811 RelA/SpoT protein

GO Term annotation Help

Process

GO:0015969 guanosine tetraphosphate metabolic process

InterPro annotation

Entry Details in BioMart

Abstract

The functions of Escherichia coli RelA and SpoT differ somewhat. RelA (EC:2.7.6.5) produces pppGpp (or ppGpp) from ATP and GTP (or GDP). SpoT (EC:3.1.7.2) degrades ppGpp, but may also act as a secondary ppGpp synthetase. The two proteins are strongly similar. In many species, a single homologue to SpoT and RelA appears reponsible for both ppGpp synthesis and ppGpp degradation.

(p)ppGpp is a regulatory metabolite of the stringent response, but appears also to be involved in antibiotic biosynthesis in some species.

Structural links Help

PDB - click here

SCOP: d.218.1.8

Database links Help

PANDIT: PF04607

Blocks: IPB007685

Pfam Clan: CL0260.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR007685

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P74007 Probable guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase

Q54089 Putative GTP pyrophosphokinase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004095	TGS
IPR002912	Amino acid-binding ACT
IPR012676	TGS-like
IPR012675	Beta-grasp fold, ferredoxin-type
IPR006674	Metal-dependent phosphohydrolase, HD subdomain
IPR004811	RelA/SpoT protein
IPR007685	RelA/SpoT
IPR003607	Metal-dependent phosphohydrolase, HD domain
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Xiao H, Kalman M, Ikehara K, Zemel S, Glaser G, Cashel M. Residual guanosine 3',5'-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations. J. Biol. Chem. 266 1991 5980-90 [PubMed: 2005134] http://intl.jbc.org/cgi/reprint/266/9/5980.pdf
	Hogg T, Mechold U, Malke H, Cashel M, Hilgenfeld R. Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response [corrected]. Cell 117 2004 57-68 [PubMed: 15066282] http://dx.doi.org/10.1016/S0092-8674(04)00260-0

InterPro 23.1