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P0AG24

- SPOT_ECOLI

UniProt

P0AG24 - SPOT_ECOLI

Protein

Bifunctional (p)ppGpp synthase/hydrolase SpoT

Gene

spoT

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
    Guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.

    Cofactori

    Manganese.

    Pathwayi

    GO - Molecular functioni

    1. amino acid binding Source: InterPro
    2. GTP diphosphokinase activity Source: UniProtKB-EC
    3. guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity Source: EcoCyc
    4. kinase activity Source: UniProtKB-KW
    5. metal ion binding Source: InterPro
    6. phosphoric diester hydrolase activity Source: InterPro
    7. protein binding Source: IntAct

    GO - Biological processi

    1. guanosine tetraphosphate biosynthetic process Source: UniProtKB-UniPathway
    2. nucleobase-containing small molecule interconversion Source: EcoCyc

    Keywords - Molecular functioni

    Hydrolase, Kinase, Transferase

    Keywords - Ligandi

    Manganese

    Enzyme and pathway databases

    BioCyciEcoCyc:SPOT-MONOMER.
    ECOL316407:JW3625-MONOMER.
    MetaCyc:SPOT-MONOMER.
    UniPathwayiUPA00908; UER00884.
    UPA00908; UER00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional (p)ppGpp synthase/hydrolase SpoT
    Including the following 2 domains:
    GTP pyrophosphokinase (EC:2.7.6.5)
    Alternative name(s):
    (p)ppGpp synthase
    ATP:GTP 3'-pyrophosphotransferase
    Stringent response-like protein
    ppGpp synthase II
    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 namesi
    Name:spoT
    Ordered Locus Names:b3650, JW3625
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10966. spoT.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Is associated with pre-50S ribosomal subunits in a salt-dependent manner.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731D → N: Obviates hydrolysis of ppGpp, moderately decreases biofilm formation, loss of biofilm induction in response to translation inhibitors. 1 Publication
    Mutagenesisi259 – 2591D → N: Obviates synthesis of ppGpp, strongly increases biofilm formation. 1 Publication
    Mutagenesisi293 – 2931D → A: Unable to restore (p)ppGpp synthesis nor complement a relA/spoT double disruption. 1 Publication
    Mutagenesisi294 – 2941Y → I: Synthesizes (p)ppGpp, complements a relA/spoT double disruption.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 702702Bifunctional (p)ppGpp synthase/hydrolase SpoTPRO_0000166569Add
    BLAST

    Proteomic databases

    PaxDbiP0AG24.
    PRIDEiP0AG24.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AG24.

    Interactioni

    Subunit structurei

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    acpPP0A6A85EBI-543228,EBI-542566

    Protein-protein interaction databases

    DIPiDIP-29378N.
    IntActiP0AG24. 59 interactions.
    MINTiMINT-1219858.
    STRINGi511145.b3650.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AG24.
    SMRiP0AG24. Positions 5-339, 387-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 144100HDAdd
    BLAST
    Domaini628 – 70275ACTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the RelA/SpoT family.Curated
    Contains 1 ACT domain.PROSITE-ProRule annotation
    Contains 1 HD domain.Curated

    Phylogenomic databases

    eggNOGiCOG0317.
    HOGENOMiHOG000018299.
    KOiK01139.
    OMAiIGYITRG.
    OrthoDBiEOG6SV551.
    PhylomeDBiP0AG24.

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR002912. 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]
    PfamiPF01966. HD. 1 hit.
    PF04607. RelA_SpoT. 1 hit.
    PF02824. TGS. 1 hit.
    [Graphical view]
    SMARTiSM00471. HDc. 1 hit.
    SM00954. RelA_SpoT. 1 hit.
    [Graphical view]
    SUPFAMiSSF81271. SSF81271. 1 hit.
    TIGRFAMsiTIGR00691. spoT_relA. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AG24-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYLFESLNQL IQTYLPEDQI KRLRQAYLVA RDAHEGQTRS SGEPYITHPV    50
    AVACILAEMK LDYETLMAAL LHDVIEDTPA TYQDMEQLFG KSVAELVEGV 100
    SKLDKLKFRD KKEAQAENFR KMIMAMVQDI RVILIKLADR THNMRTLGSL 150
    RPDKRRRIAR ETLEIYSPLA HRLGIHHIKT ELEELGFEAL YPNRYRVIKE 200
    VVKAARGNRK EMIQKILSEI EGRLQEAGIP CRVSGREKHL YSIYCKMVLK 250
    EQRFHSIMDI YAFRVIVNDS DTCYRVLGQM HSLYKPRPGR VKDYIAIPKA 300
    NGYQSLHTSM IGPHGVPVEV QIRTEDMDQM AEMGVAAHWA YKEHGETSTT 350
    AQIRAQRWMQ SLLELQQSAG SSFEFIESVK SDLFPDEIYV FTPEGRIVEL 400
    PAGATPVDFA YAVHTDIGHA CVGARVDRQP YPLSQPLTSG QTVEIITAPG 450
    ARPNAAWLNF VVSSKARAKI RQLLKNLKRD DSVSLGRRLL NHALGGSRKL 500
    NEIPQENIQR ELDRMKLATL DDLLAEIGLG NAMSVVVAKN LQHGDASIPP 550
    ATQSHGHLPI KGADGVLITF AKCCRPIPGD PIIAHVSPGK GLVIHHESCR 600
    NIRGYQKEPE KFMAVEWDKE TAQEFITEIK VEMFNHQGAL ANLTAAINTT 650
    TSNIQSLNTE EKDGRVYSAF IRLTARDRVH LANIMRKIRV MPDVIKVTRN 700
    RN 702
    Length:702
    Mass (Da):79,342
    Last modified:December 20, 2005 - v1
    Checksum:iA85F70F57D082EE8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24503 Genomic DNA. Translation: AAB00160.1.
    L10328 Genomic DNA. Translation: AAA62003.1.
    U00096 Genomic DNA. Translation: AAC76674.1.
    AP009048 Genomic DNA. Translation: BAE77643.1.
    PIRiB30374. SHECGD.
    RefSeqiNP_418107.1. NC_000913.3.
    YP_491784.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76674; AAC76674; b3650.
    BAE77643; BAE77643; BAE77643.
    GeneIDi12930367.
    948159.
    KEGGiecj:Y75_p3524.
    eco:b3650.
    PATRICi32122787. VBIEscCol129921_3770.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24503 Genomic DNA. Translation: AAB00160.1 .
    L10328 Genomic DNA. Translation: AAA62003.1 .
    U00096 Genomic DNA. Translation: AAC76674.1 .
    AP009048 Genomic DNA. Translation: BAE77643.1 .
    PIRi B30374. SHECGD.
    RefSeqi NP_418107.1. NC_000913.3.
    YP_491784.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0AG24.
    SMRi P0AG24. Positions 5-339, 387-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29378N.
    IntActi P0AG24. 59 interactions.
    MINTi MINT-1219858.
    STRINGi 511145.b3650.

    Proteomic databases

    PaxDbi P0AG24.
    PRIDEi P0AG24.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76674 ; AAC76674 ; b3650 .
    BAE77643 ; BAE77643 ; BAE77643 .
    GeneIDi 12930367.
    948159.
    KEGGi ecj:Y75_p3524.
    eco:b3650.
    PATRICi 32122787. VBIEscCol129921_3770.

    Organism-specific databases

    EchoBASEi EB0959.
    EcoGenei EG10966. spoT.

    Phylogenomic databases

    eggNOGi COG0317.
    HOGENOMi HOG000018299.
    KOi K01139.
    OMAi IGYITRG.
    OrthoDBi EOG6SV551.
    PhylomeDBi P0AG24.

    Enzyme and pathway databases

    UniPathwayi UPA00908 ; UER00884 .
    UPA00908 ; UER00886 .
    BioCyci EcoCyc:SPOT-MONOMER.
    ECOL316407:JW3625-MONOMER.
    MetaCyc:SPOT-MONOMER.

    Miscellaneous databases

    PROi P0AG24.

    Gene expression databases

    Genevestigatori P0AG24.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR002912. 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 ]
    Pfami PF01966. HD. 1 hit.
    PF04607. RelA_SpoT. 1 hit.
    PF02824. TGS. 1 hit.
    [Graphical view ]
    SMARTi SM00471. HDc. 1 hit.
    SM00954. RelA_SpoT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81271. SSF81271. 1 hit.
    TIGRFAMsi TIGR00691. spoT_relA. 1 hit.
    PROSITEi PS51671. ACT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiSPOT_ECOLI
    AccessioniPrimary (citable) accession number: P0AG24
    Secondary accession number(s): P17580, Q2M7W3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3