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P0A0F0

- RELA_STAAU

UniProt

P0A0F0 - RELA_STAAU

Protein

GTP pyrophosphokinase

Gene

relA

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (15 Feb 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 formation of pppGpp which is then hydrolyzed to form ppGpp By similarity.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
    6. metal ion binding Source: InterPro
    7. phosphoric diester hydrolase activity Source: InterPro

    GO - Biological processi

    1. guanosine tetraphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Transferase

    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
    Synonyms:rel
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 736736GTP pyrophosphokinasePRO_0000166559Add
    BLAST

    Proteomic databases

    PRIDEiP0A0F0.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A0F0.
    SMRiP0A0F0. Positions 14-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 156100HDAdd
    BLAST
    Domaini662 – 73675ACTPROSITE-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.

    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]
    PfamiPF01842. ACT. 1 hit.
    PF01966. 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.

    P0A0F0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGVYHIMNN EYPYSADEVL HKAKSYLSAD EYEYVLKSYH IAYEAHKGQF    50
    RKNGLPYIMH PIQVAGILTE MRLDGPTIVA GFLHDVIEDT PYTFEDVKEM 100
    FNEEVARIVD GVTKLKKVKY RSKEEQQAEN HRKLFIAIAK DVRVILVKLA 150
    DRLHNMRTLK AMPREKQIRI SRETLEIYAP LAHRLGINTI KWELEDTALR 200
    YIDNVQYFRI VNLMKKKRSE REAYIETAID RIRTEMDRMN IEGDINGRPK 250
    HIYSIYRKMM KQKKQFDQIF DLLAIRVIVN SINDCYAILG LVHTLWKPMP 300
    GRFKDYIAMP KQNLYQSLHT TVVGPNGDPL EIQIRTFDMH EIAEHGVAAH 350
    WAYKEGKKVS EKDQTYQNKL NWLKELAEAD HTSSDAQEFM ETLKYDLQSD 400
    KVYAFTPASD VIELPYGAVP IDFAYAIHSE VGNKMIGAKV NGKIVPIDYI 450
    LQTGDIVEIR TSKHSYGPSR DWLKIVKSSS AKGKIKSFFK KQDRSSNIEK 500
    GRMMVEVEIK EQGFRVEDIL TEKNIQVVNE KYNFANEDDL FAAVGFGGVT 550
    SLQIVNKLTE RQRILDKQRA LNEAQEVTKS LPIKDNIITD SGVYVEGLEN 600
    VLIKLSKCCN PIPGDDIVGY ITKGHGIKVH RTDCPNIKNE TERLINVEWV 650
    KSKDATQKYQ VDLEVTAYDR NGLLNEVLQA VSSTAGNLIK VSGRSDIDKN 700
    AIINISVMVK NVNDVYRVVE KIKQLGDVYT VTRVWN 736
    Length:736
    Mass (Da):84,537
    Last modified:February 15, 2005 - v1
    Checksum:iC1EC881D00431801
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D76414 Genomic DNA. Translation: BAA23138.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D76414 Genomic DNA. Translation: BAA23138.1 .

    3D structure databases

    ProteinModelPortali P0A0F0.
    SMRi P0A0F0. Positions 14-357.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P0A0F0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0317.

    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.
    IPR006674. HD_domain.
    IPR004811. RelA/Spo_fam.
    IPR007685. RelA_SpoT.
    IPR004095. TGS.
    IPR012676. TGS-like.
    [Graphical view ]
    Pfami PF01842. ACT. 1 hit.
    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. "Increase of methicillin resistance in Staphylococcus aureus caused by deletion of a gene whose product is homologous to lytic enzymes."
      Fujimura T., Murakami K.
      J. Bacteriol. 179:6294-6301(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SR17238.

    Entry informationi

    Entry nameiRELA_STAAU
    AccessioniPrimary (citable) accession number: P0A0F0
    Secondary accession number(s): O32419
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 57 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