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P0AG24 (SPOT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional (p)ppGpp synthase/hydrolase SpoT

Including the following 2 domains:

  1. GTP pyrophosphokinase
    EC=2.7.6.5
    Alternative name(s):
    (p)ppGpp synthase
    ATP:GTP 3'-pyrophosphotransferase
    Stringent response-like protein
    ppGpp synthase II
  2. Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase
    EC=3.1.7.2
    Alternative name(s):
    Penta-phosphate guanosine-3'-pyrophosphohydrolase
    Short name=(ppGpp)ase
Gene names
Name:spoT
Ordered Locus Names:b3650, JW3625
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length702 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the synthesis and degradation of ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c-di-GMP induces it. Ref.7 Ref.10

Catalytic activity

ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.

Guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.

Cofactor

Manganese.

Pathway

Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1.

Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2.

Subunit structure

Interacts with ObgE/CgtA (AC P42641); this association is not required for pre-50S ribosome binding. Under both amino acid and carbon starvation conditions about half of the protein dissociates from the ribosome. Ref.8 Ref.9

Subcellular location

Cytoplasm. Note: Is associated with pre-50S ribosomal subunits in a salt-dependent manner. Ref.9

Disruption phenotype

In the presence of wild-type relA, spoT cannot be deleted because ppGpp accumulation is toxic. In the double relA/spoT deletion (a ppGpp0 mutant) there is a very large increase in biofilm formation (in a csrA-disrupted background). The double relA/spoT deletion obviates persister cell formation in a hipA7 mutant. Ref.7 Ref.10

Sequence similarities

Belongs to the RelA/SpoT family.

Contains 1 ACT domain.

Contains 1 HD domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

acpPP0A6A85EBI-543228,EBI-542566

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 702702Bifunctional (p)ppGpp synthase/hydrolase SpoT
PRO_0000166569

Regions

Domain45 – 144100HD
Domain628 – 70275ACT

Experimental info

Mutagenesis731D → N: Obviates hydrolysis of ppGpp, moderately decreases biofilm formation, loss of biofilm induction in response to translation inhibitors. Ref.10
Mutagenesis2591D → N: Obviates synthesis of ppGpp, strongly increases biofilm formation. Ref.10
Mutagenesis2931D → A: Unable to restore (p)ppGpp synthesis nor complement a relA/spoT double disruption. Ref.6
Mutagenesis2941Y → I: Synthesizes (p)ppGpp, complements a relA/spoT double disruption.

Sequences

Sequence LengthMass (Da)Tools
P0AG24 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: A85F70F57D082EE8

FASTA70279,342
        10         20         30         40         50         60 
MYLFESLNQL IQTYLPEDQI KRLRQAYLVA RDAHEGQTRS SGEPYITHPV AVACILAEMK 

        70         80         90        100        110        120 
LDYETLMAAL LHDVIEDTPA TYQDMEQLFG KSVAELVEGV SKLDKLKFRD KKEAQAENFR 

       130        140        150        160        170        180 
KMIMAMVQDI RVILIKLADR THNMRTLGSL RPDKRRRIAR ETLEIYSPLA HRLGIHHIKT 

       190        200        210        220        230        240 
ELEELGFEAL YPNRYRVIKE VVKAARGNRK EMIQKILSEI EGRLQEAGIP CRVSGREKHL 

       250        260        270        280        290        300 
YSIYCKMVLK EQRFHSIMDI YAFRVIVNDS DTCYRVLGQM HSLYKPRPGR VKDYIAIPKA 

       310        320        330        340        350        360 
NGYQSLHTSM IGPHGVPVEV QIRTEDMDQM AEMGVAAHWA YKEHGETSTT AQIRAQRWMQ 

       370        380        390        400        410        420 
SLLELQQSAG SSFEFIESVK SDLFPDEIYV FTPEGRIVEL PAGATPVDFA YAVHTDIGHA 

       430        440        450        460        470        480 
CVGARVDRQP YPLSQPLTSG QTVEIITAPG ARPNAAWLNF VVSSKARAKI RQLLKNLKRD 

       490        500        510        520        530        540 
DSVSLGRRLL NHALGGSRKL NEIPQENIQR ELDRMKLATL DDLLAEIGLG NAMSVVVAKN 

       550        560        570        580        590        600 
LQHGDASIPP ATQSHGHLPI KGADGVLITF AKCCRPIPGD PIIAHVSPGK GLVIHHESCR 

       610        620        630        640        650        660 
NIRGYQKEPE KFMAVEWDKE TAQEFITEIK VEMFNHQGAL ANLTAAINTT TSNIQSLNTE 

       670        680        690        700 
EKDGRVYSAF IRLTARDRVH LANIMRKIRV MPDVIKVTRN RN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the spoT gene of Escherichia coli."
Sarubbi E., Rudd K.E., Xiao H., Ikehara K., Kalman M., Cashel M.
J. Biol. Chem. 264:15074-15082(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Residual guanosine 3',5'-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations."
Xiao H., Kalman M., Ikehara K., Zemel S., Glaser G., Cashel M.
J. Biol. Chem. 266:5980-5990(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE (P)PPGPP SYNTHESIS ACTIVITY.
[6]"Identification of an indispensable amino acid for ppGpp synthesis of Escherichia coli SpoT protein."
Fujita C., Maeda M., Fujii T., Iwamoto R., Ikehara K.
Biosci. Biotechnol. Biochem. 66:2735-2738(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PPGPP SYNTHASE ACTIVITY, MUTAGENESIS OF ASP-293.
Strain: CF8295.
[7]"Characterization of the hipA7 allele of Escherichia coli and evidence that high persistence is governed by (p)ppGpp synthesis."
Korch S.B., Henderson T.A., Hill T.M.
Mol. Microbiol. 50:1199-1213(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PERSISTENCE, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
[8]"The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase."
Wout P., Pu K., Sullivan S.M., Reese V., Zhou S., Lin B., Maddock J.R.
J. Bacteriol. 186:5249-5257(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OBGE/CGTA.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]"G-protein control of the ribosome-associated stress response protein SpoT."
Jiang M., Sullivan S.M., Wout P.K., Maddock J.R.
J. Bacteriol. 189:6140-6147(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, LARGE RIBOSOMAL SUBUNIT ASSOCIATION, CHARACTERIZATION UNDER AMINO ACID OR CARBON STARVATION.
Strain: K12.
[10]"Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress."
Boehm A., Steiner S., Zaehringer F., Casanova A., Hamburger F., Ritz D., Keck W., Ackermann M., Schirmer T., Jenal U.
Mol. Microbiol. 72:1500-1516(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN BIOFILM FORMATION, MUTAGENESIS OF ASP-73 AND ASP-259, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / AB400.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24503 Genomic DNA. Translation: AAB00160.1.
L10328 Genomic DNA. Translation: AAA62003.1.
U00096 Genomic DNA. Translation: AAC76674.1.
AP009048 Genomic DNA. Translation: BAE77643.1.
PIRSHECGD. B30374.
RefSeqNP_418107.1. NC_000913.3.
YP_491784.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AG24.
SMRP0AG24. Positions 5-339, 387-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29378N.
IntActP0AG24. 59 interactions.
MINTMINT-1219858.
STRING511145.b3650.

Proteomic databases

PaxDbP0AG24.
PRIDEP0AG24.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76674; AAC76674; b3650.
BAE77643; BAE77643; BAE77643.
GeneID12930367.
948159.
KEGGecj:Y75_p3524.
eco:b3650.
PATRIC32122787. VBIEscCol129921_3770.

Organism-specific databases

EchoBASEEB0959.
EcoGeneEG10966. spoT.

Phylogenomic databases

eggNOGCOG0317.
HOGENOMHOG000018299.
KOK01139.
OMAIGYITRG.
OrthoDBEOG6SV551.
PhylomeDBP0AG24.

Enzyme and pathway databases

BioCycEcoCyc:SPOT-MONOMER.
ECOL316407:JW3625-MONOMER.
MetaCyc:SPOT-MONOMER.
UniPathwayUPA00908; UER00884.
UPA00908; UER00886.

Gene expression databases

GenevestigatorP0AG24.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR002912. ACT_dom.
IPR012675. Beta-grasp_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR004811. RelA/Spo_fam.
IPR007685. RelA_SpoT.
IPR004095. TGS.
IPR012676. TGS-like.
[Graphical view]
PfamPF01966. HD. 1 hit.
PF04607. RelA_SpoT. 1 hit.
PF02824. TGS. 1 hit.
[Graphical view]
SMARTSM00471. HDc. 1 hit.
SM00954. RelA_SpoT. 1 hit.
[Graphical view]
SUPFAMSSF81271. SSF81271. 1 hit.
TIGRFAMsTIGR00691. spoT_relA. 1 hit.
PROSITEPS51671. ACT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP0AG24.

Entry information

Entry nameSPOT_ECOLI
AccessionPrimary (citable) accession number: P0AG24
Secondary accession number(s): P17580, Q2M7W3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene