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P55133

- RELA_PHOAS

UniProt

P55133 - RELA_PHOAS

Protein

GTP pyrophosphokinase

Gene

relA

Organism
Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 / CCUG 15956))
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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. Plays also a role in the reductive division that occurs during the initial phase of nutrient starvation.

    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. 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
    OrganismiPhotobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 / CCUG 15956))
    Taxonomic identifieri314292 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

    Pathology & Biotechi

    Disruption phenotypei

    Mutants remain rod shaped, and do not acquire the typical coccoid morphology usually seen during starvation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 744744GTP pyrophosphokinasePRO_0000166566Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP55133.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini669 – 74476ACTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR012675. Beta-grasp_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]
    SMARTiSM00954. 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.

    P55133-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVAVRGAHLK ENTTFELVSW VESLRQDAKV SSRIEGTYQR CIELAAEQEN    50
    GPLLLWRGRE LVEILVTLSM DADTLIAALL YPLVEGGCYS TDALKEEYSG 100
    TILHLVQGVE QMCAISQLKS TAEETAQAAQ VDNIRRMLLS MVDDFRCVVI 150
    KLAERICNLR EVKDQPDEVR RAAAQECANI YAPLANRLGI GQLKWEIEDY 200
    AFRYQHPDTY KQIAKQLSER RIDREDYITH FVDDLSDAMK ASNIRAEVQG 250
    RPKHIYSIWR KMQKKSLEFD ELFDVRAVRI VAEELQDCYA ALGVVHTKYR 300
    HLPKEFDDYV ANPKPNGYQS IHTVVLGPEG KTIEIQIRTK QMHEESELGV 350
    AAHWKYKEGT ASGGAQSAYD EKINWLRKLL AWQEEMSDSG EMLDELRSQV 400
    FDDRVYAFTP KGDVVDLPSN ATPLDFAYHI HSEVGHRCIG AKVEGRIVPF 450
    TYHLQMGDQV EIITQKEPNP SRDWLNPNLG FVTSSRARAK VHAWFRKQDR 500
    DKNIIAGKEI LEAELVKIHA TLKDAQYYAA KRFNVKSPEE LYAGIGSGDL 550
    RINQVINHIN ALVNKPTAEE EDQQLLEKLS EASNKQATSH KKPQRDAVVV 600
    EGVDNLMTHL ARCCQPIPGD DIQGFVTQGR GISVHRMDCE QLEELRHHAP 650
    ERIIDTVWGG GFVGNYTITV RVTASERNGL LKELTNTLMN EKVKVAGMKS 700
    RVDYKKQMSI MDFELELTDL EVLGRVLKRI EQVKDVAEAK RLYG 744
    Length:744
    Mass (Da):84,546
    Last modified:October 1, 1996 - v1
    Checksum:iB7AC772C4D47A40C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13769 Genomic DNA. Translation: AAA62208.1.

    Genome annotation databases

    PATRICi31352187. VBIPhoAng36222_3707.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13769 Genomic DNA. Translation: AAA62208.1 .

    3D structure databases

    ProteinModelPortali P55133.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    PATRICi 31352187. VBIPhoAng36222_3707.

    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.
    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 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. "Stringent control during carbon starvation of marine Vibrio sp. strain S14: molecular cloning, nucleotide sequence, and deletion of the relA gene."
      Flaerdh K., Axberg T., Albertson N.H., Kjelleberg S.
      J. Bacteriol. 176:5949-5957(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiRELA_PHOAS
    AccessioniPrimary (citable) accession number: P55133
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 79 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