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P0AG25

- SPOT_ECO57

UniProt

P0AG25 - SPOT_ECO57

Protein

Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase

Gene

spoT

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (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 the degradation of ppGpp into GDP. It may also be capable of catalyzing the synthesis of ppGpp By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Manganese.By similarity

    Pathwayi

    GO - Molecular functioni

    1. amino acid binding Source: InterPro
    2. guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity Source: UniProtKB-EC
    3. metal ion binding Source: InterPro
    4. phosphoric diester hydrolase activity Source: InterPro

    GO - Biological processi

    1. guanosine tetraphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Manganese

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-4493-MONOMER.
    ECOO157:SPOT-MONOMER.
    UniPathwayiUPA00908; UER00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    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:Z5076, ECs4525
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 702702Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolasePRO_0000166570Add
    BLAST

    Proteomic databases

    PRIDEiP0AG25.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1219842.
    STRINGi155864.Z5076.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AG25.
    SMRiP0AG25. 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.

    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.

    P0AG25-1 [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
    AE005174 Genomic DNA. Translation: AAG58794.1.
    BA000007 Genomic DNA. Translation: BAB37948.1.
    PIRiE91194.
    F86041.
    RefSeqiNP_290230.1. NC_002655.2.
    NP_312552.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG58794; AAG58794; Z5076.
    BAB37948; BAB37948; BAB37948.
    GeneIDi915518.
    960895.
    KEGGiece:Z5076.
    ecs:ECs4525.
    PATRICi18358673. VBIEscCol44059_4502.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG58794.1 .
    BA000007 Genomic DNA. Translation: BAB37948.1 .
    PIRi E91194.
    F86041.
    RefSeqi NP_290230.1. NC_002655.2.
    NP_312552.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P0AG25.
    SMRi P0AG25. Positions 5-339, 387-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1219842.
    STRINGi 155864.Z5076.

    Proteomic databases

    PRIDEi P0AG25.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG58794 ; AAG58794 ; Z5076 .
    BAB37948 ; BAB37948 ; BAB37948 .
    GeneIDi 915518.
    960895.
    KEGGi ece:Z5076.
    ecs:ECs4525.
    PATRICi 18358673. VBIEscCol44059_4502.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00908 ; UER00886 .
    BioCyci ECOL386585:GJFA-4493-MONOMER.
    ECOO157:SPOT-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiSPOT_ECO57
    AccessioniPrimary (citable) accession number: P0AG25
    Secondary accession number(s): P17580
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 72 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3