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O85709

- RELA_STRAT

UniProt

O85709 - RELA_STRAT

Protein

GTP pyrophosphokinase

Gene

relA

Organism
Streptomyces antibioticus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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 formation of pppGpp which is then hydrolyzed to form ppGpp By similarity. Is required for actinomycin production.By similarity

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. amino acid binding Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. GTP binding Source: UniProtKB-KW
    4. GTP diphosphokinase activity Source: UniProtKB-EC
    5. kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. antibiotic biosynthetic process Source: UniProtKB-KW
    2. guanosine tetraphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    ATP-binding, GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00908; UER00884.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP pyrophosphokinase (EC:2.7.6.5)
    Alternative name(s):
    (p)ppGpp synthase
    ATP:GTP 3'-pyrophosphotransferase
    ppGpp synthase I
    Gene namesi
    Name:relA
    OrganismiStreptomyces antibioticus
    Taxonomic identifieri1890 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 841841GTP pyrophosphokinasePRO_0000166563Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO85709.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini146 – 24398HDAdd
    BLAST
    Domaini763 – 83775ACTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR012675. Beta-grasp_dom.
    IPR003607. HD/PDEase_dom.
    IPR004811. RelA/Spo_fam.
    IPR007685. RelA_SpoT.
    IPR004095. TGS.
    IPR012676. TGS-like.
    [Graphical view]
    PfamiPF01842. ACT. 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.

    O85709-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPDEAQHLTA AKPDSAAGAA AEPAAHAQDG GGPVEHDRSA PADKPAERTR    50
    PKPAPPERPR PPPPRARAAG QPAARSGGSS NRVRARLARL GVQRANLTHP 100
    VLEPLLRIVR ANDPKIETST LRQIEKAYQV AERWHRGQKR KSGDPYITHP 150
    LAVTTILAEL GMDPATLMAG LLHDSREDTE YGLDDLRRDF GDVVGLLVDG 200
    VTKLDKVKFG EAAQAETVRK MVVAMAKDPR VLVIKLADRL HNMRTMRYLK 250
    REKQEKKARE TLEIYAPLAH RLGMNTIKWE LEDLAFAILY PKMYDEIVRL 300
    VAERAPKRDE YLAIVTDEVQ SDLRARRIKA TVTGRPKHYY SVYQKIIVRG 350
    RDFAEIYDLV GIRVLVDTVR DCYAALGTVH ARWNPVPGRF KDYIAMPKFN 400
    MYQSLHTTVI GPNGKPVELQ IRTFDMHRRA EYGIAAHWKY KQEAVARASK 450
    VRTDVPKPAK GKDDHLNDMA WLRQLLDWQK ETEDPGEFLE SLRFDLSRNE 500
    VFVFTPKSDV IALPAGATPV DFAYAVHTEV GHRTIGARVN GRLVPLESTL 550
    DNGDLVEVFT SKAAGAGPSR DWLGFVKSPR ARNKIRAWFS KERRDEAIEQ 600
    GKDAIARAMR KQNLPIQRIL TGDSLVTLAH EMRYPDISSS DAAIGEGHVG 650
    AQNVVQKLVQ ALGGEEAASE EIDEAVPSRS RSRKRRSNQD PGVVVKGVDD 700
    VWVKLARCCT PVPGEPIIGF VTRGSAVSVH RSDCVNVESL AREPERILEV 750
    EWAPTQSSVF LVAIQVEALD RSRLLSDVTR VLSDQHVNIL SAAVQTSRDR 800
    VATSRFTFEM GDPKHLGHVL KAVRGVEGVY DVYRVTPGPQ P 841
    Length:841
    Mass (Da):93,672
    Last modified:November 1, 1998 - v1
    Checksum:i632A037BA4EF4C94
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072829 Genomic DNA. Translation: AAC26021.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072829 Genomic DNA. Translation: AAC26021.1 .

    3D structure databases

    ProteinModelPortali O85709.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00908 ; UER00884 .

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR002912. ACT_dom.
    IPR012675. Beta-grasp_dom.
    IPR003607. HD/PDEase_dom.
    IPR004811. RelA/Spo_fam.
    IPR007685. RelA_SpoT.
    IPR004095. TGS.
    IPR012676. TGS-like.
    [Graphical view ]
    Pfami PF01842. ACT. 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. "relA is required for actinomycin production in Streptomyces antibioticus."
      Hoyt S., Jones G.H.
      J. Bacteriol. 181:3824-3829(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 41481 / IMRU 3720.

    Entry informationi

    Entry nameiRELA_STRAT
    AccessioniPrimary (citable) accession number: O85709
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1998
    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

    Documents

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

    External Data

    Dasty 3