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Q54089

- RELA_STREQ

UniProt

Q54089 - RELA_STREQ

Protein

Bifunctional (p)ppGpp synthase/hydrolase RelA

Gene

relA

Organism
Streptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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 both the formation of pppGpp which is then hydrolyzed to form ppGpp, and the hydrolysis of ppGpp. The enzyme does not simultaneously display both synthase and hydrolase activities. In the structure of residues 1-385 there are 2 conformations seen, the hydrolase-OFF/synthase-ON and hydrolase-ON/synthase-OFF, suggesting there is ligand-induced signal transmission between the 2 active sites.

    Catalytic activityi

    ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
    Guanosine 3',5'-bis(diphosphate) + H2O = guanosine 5'-diphosphate + diphosphate.

    Cofactori

    Binds 1 Mg2+ per subunit.Curated
    Binds 1 Mn2+ per subunit.1 Publication

    Enzyme regulationi

    Alpha-beta methylenyl ATP, an ATP-analog inhibitor of the synthase activity also reduces the hydrolase activity about 4-fold.2 Publications

    Kineticsi

    1. KM=2 mM for GTP1 Publication
    2. KM=5 mM for ATP1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531Manganese
    Metal bindingi77 – 771Manganese
    Active sitei81 – 811Nucleophile, for hydrolase activitySequence Analysis
    Active sitei82 – 821Nucleophile, for hydrolase activitySequence Analysis
    Metal bindingi144 – 1441Manganese
    Metal bindingi264 – 2641MagnesiumSequence Analysis

    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. guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity Source: UniProtKB-EC
    6. kinase activity Source: UniProtKB-KW
    7. metal ion binding Source: UniProtKB-KW
    8. phosphoric diester hydrolase activity Source: InterPro

    GO - Biological processi

    1. guanosine tetraphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase, Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, GTP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ54089.
    UniPathwayiUPA00908; UER00884.
    UPA00908; UER00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional (p)ppGpp synthase/hydrolase RelA
    Including the following 2 domains:
    GTP pyrophosphokinase (EC:2.7.6.5)
    Alternative name(s):
    (p)ppGpp synthase
    ATP:GTP 3'-pyrophosphotransferase
    Stringent response-like protein
    ppGpp synthase I
    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:relA
    Synonyms:rel
    OrganismiStreptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis)
    Taxonomic identifieri119602 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441R → Q: No hydrolase activity. 1 Publication
    Mutagenesisi78 – 781D → A: No hydrolase activity. 1 Publication
    Mutagenesisi81 – 811E → G: No hydrolase activity. 1 Publication
    Mutagenesisi82 – 821D → V: No hydrolase activity. 1 Publication
    Mutagenesisi151 – 1511T → A or P: No hydrolase activity. 1 Publication
    Mutagenesisi264 – 2641D → G: No synthase activity. 1 Publication
    Mutagenesisi323 – 3231E → Q: No synthase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 739739Bifunctional (p)ppGpp synthase/hydrolase RelAPRO_0000166565Add
    BLAST

    Structurei

    Secondary structure

    1
    739
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1911
    Helixi22 – 3817
    Turni39 – 413
    Helixi52 – 6312
    Helixi68 – 769
    Helixi79 – 824
    Helixi87 – 948
    Helixi96 – 10813
    Turni128 – 1303
    Helixi135 – 15016
    Helixi160 – 16910
    Helixi171 – 1777
    Helixi181 – 19515
    Helixi197 – 20913
    Helixi211 – 23020
    Turni231 – 2333
    Beta strandi237 – 2404
    Helixi245 – 25511
    Helixi256 – 2583
    Helixi263 – 2653
    Beta strandi267 – 2748
    Helixi275 – 28814
    Turni299 – 3013
    Beta strandi311 – 3166
    Beta strandi318 – 32811
    Helixi329 – 3379
    Helixi364 – 3707

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VJ7X-ray2.10A/B1-385[»]
    ProteinModelPortaliQ54089.
    SMRiQ54089. Positions 5-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ54089.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 149100HDAdd
    BLAST
    Domaini664 – 73976ACTPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Based on a random mutagenesis study of the catalytic fragment (residues 1-385), the (p)ppGpp phosphohydrolase domain seems to encompass approximately the first 225 residues, while the (p)ppGpp synthase domain seems to be found between residues 226 and 385.

    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.

    Q54089-1 [UniParc]FASTAAdd to Basket

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    MAKEINLTGE EVVALAAKYM NETDAAFVKK ALDYATAAHF YQVRKSGEPY    50
    IVHPIQVAGI LADLHLDAVT VACGFLHDVV EDTDITLDNI EFDFGKDVRD 100
    IVDGVTKLGK VEYKSHEEQL AENHRKMLMA MSKDIRVILV KLADRLHNMR 150
    TLKHLRKDKQ ERISRETMEI YAPLAHRLGI SRIKWELEDL AFRYLNETEF 200
    YKISHMMNEK RREREALVDD IVTKIKSYTT EQGLFGDVYG RPKHIYSIYR 250
    KMRDKKKRFD QIFDLIAIRC VMETQSDVYA MVGYIHELWR PMPGRFKDYI 300
    AAPKANGYQS IHTTVYGPKG PIEIQIRTKE MHQVAEYGVA AHWAYKKGVR 350
    GKVNQAEQKV GMNWIKELVE LQDASNGDAV DFVDSVKEDI FSERIYVFTP 400
    TGAVQELPKD SGPIDFAYAI HTQVGEKAIG AKVNGRMVPL TAKLKTGDVV 450
    EIVTNPNSFG PSRDWIKLVK TNKARNKIRQ FFKNQDKELS VNKGRDMLVS 500
    YFQEQGYVAN KYLDKKRIEA ILPKVSVKSE ESLYAAVGFG DISPVSVFNK 550
    LTEKERREEE RAKAKAEAEE LVNGGEIKHE NKDVLKVRSE NGVIIQGASG 600
    LLMRIAKCCN PVPGDPIEGY ITKGRGIAIH RADCNNIKSQ DGYQERLIEV 650
    EWDLDNSSKD YQAEIDIYGL NRRGLLNDVL QILSNSTKSI STVNAQPTKD 700
    MKFANIHVSF GIPNLTHLTT VVEKIKAVPD VYSVKRTNG 739
    Length:739
    Mass (Da):83,913
    Last modified:November 1, 1997 - v1
    Checksum:iE65CBEF99103D171
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72832 Genomic DNA. Translation: CAA51353.1.
    PIRiS39975.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72832 Genomic DNA. Translation: CAA51353.1 .
    PIRi S39975.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VJ7 X-ray 2.10 A/B 1-385 [» ]
    ProteinModelPortali Q54089.
    SMRi Q54089. Positions 5-371.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1163118.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00908 ; UER00884 .
    UPA00908 ; UER00886 .
    SABIO-RK Q54089.

    Miscellaneous databases

    EvolutionaryTracei Q54089.

    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. "Genetic organization of the streptokinase region of the Streptococcus equisimilis H46A chromosome."
      Mechold U., Steiner K., Vettermann S., Malke H.
      Mol. Gen. Genet. 241:129-140(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: H46A.
    2. "Intramolecular regulation of the opposing (p)ppGpp catalytic activities of Rel(Seq), the Rel/Spo enzyme from Streptococcus equisimilis."
      Mechold U., Murphy H., Brown L., Cashel M.
      J. Bacteriol. 184:2878-2888(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    3. "Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response."
      Hogg T., Mechold U., Malke H., Cashel M., Hilgenfeld R.
      Cell 117:57-68(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-385 BOUND TO GUANOSINE-NUCLEOTIDE DERIVATIVES, HYDROLASE AND SYNTHASE ACTIVITIES, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF ARG-44; ASP-78; GLU-81; ASP-82; THR-151; ASP-264 AND GLU-323.
      Strain: H46A.

    Entry informationi

    Entry nameiRELA_STREQ
    AccessioniPrimary (citable) accession number: Q54089
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 91 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

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3