Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O34098

- SPOT_SPICI

UniProt

O34098 - SPOT_SPICI

Protein

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

Gene

spoT

Organism
Spiroplasma citri
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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
    OrganismiSpiroplasma citri
    Taxonomic identifieri2133 [NCBI]
    Taxonomic lineageiBacteriaTenericutesMollicutesEntomoplasmatalesSpiroplasmataceaeSpiroplasma

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 749749Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolasePRO_0000166575Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliO34098.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 148100HDAdd
    BLAST
    Domaini674 – 74976ACTPROSITE-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.
    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.

    O34098-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRDIKYEEV LAQIKLYIKD EATLKEIQKA YEYAEEKHHG QVRNSGARYI    50
    IHPLWTTFFL AQWRMGPKTL IAGLLHDVLE DTPATFEELQ ELFGIEIANL 100
    VEGVTKVSYF AKENRTQIKA QYLRKLYLSM AKDIRVIIVK LADRLHNLKT 150
    IGYLKPERQQ IIARESLEIY SAIAHRLGMK AVKQEIEDIS FKIINPVQYN 200
    KIVSLLESSN KERENTINQK IEELKKILIT EKKMSVKVYG RSKSIYSIYR 250
    KMNQFGKNFD DIHDILAVRI ITNSVDDCYK VLGFVHQHYT PLNNRFKDYI 300
    ATPKHNLYQS LHTTIVADDG LIFEVQIRTE EMDELAEQGV AAHWRYKEGE 350
    NYDIAKKQKD IDERLDIFKR ILDLENISVQ ERDEIQQEVY KPDHLMEQII 400
    QNDIFSSLIY VLTPNGKVVT LPFGSTVLDF AYKIHSEIGE KTIGAKINGL 450
    FSPISTVLKS GDVVDIKTAA TQKPNHSWLV VSKTSSALEK IKKYLKKELV 500
    EVTSDAKSVN LEKIKQTKSQ IEEYIAKKDL KWKLVNSETQ LERLHAINFN 550
    NIEDFLLDVA NDEYTLEEAI NLVYLDHETS QNEKILKKLQ DKQYKKAQLK 600
    DDIIVQGISN IKVVISQCCL PIPYEDITGY VSKAEGIKVH LKTCRNIQSG 650
    DKQDRQVEVS WNEAVCKNKQ YDCAIRIEAI DRPALLVDVT KVLSHLNASV 700
    QMMSANVSGD LMNLTIKTII KVSNADRLQQ IRSSLLTIPD IKVVERVMM 749
    Length:749
    Mass (Da):86,282
    Last modified:January 1, 1998 - v1
    Checksum:iD32992E612317042
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89875 Genomic DNA. Translation: AAC45548.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89875 Genomic DNA. Translation: AAC45548.1 .

    3D structure databases

    ProteinModelPortali O34098.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00908 ; UER00886 .

    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. "Isolation, characterization, and complementation of a motility mutant of Spiroplasma citri."
      Jacob C., Nouzieres F., Duret S., Bove J.M., Renaudin J.
      J. Bacteriol. 179:4802-4810(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: GII-3.

    Entry informationi

    Entry nameiSPOT_SPICI
    AccessioniPrimary (citable) accession number: O34098
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 82 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