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Protein

Bifunctional (p)ppGpp synthase/hydrolase RelA

Gene

relA

Organism
Streptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:
  • Mg2+CuratedNote: Binds 1 Mg2+ ion per subunit.Curated
  • Mn2+1 PublicationNote: Binds 1 Mn2+ ion per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ppGpp biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes ppGpp from GDP.
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional (p)ppGpp synthase/hydrolase RelA (relA)
    This subpathway is part of the pathway ppGpp biosynthesis, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes ppGpp from GDP, the pathway ppGpp biosynthesis and in Purine metabolism.

    Pathwayi: ppGpp biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes ppGpp from GTP.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Bifunctional (p)ppGpp synthase/hydrolase RelA (relA)
    2. no protein annotated in this organism
    This subpathway is part of the pathway ppGpp biosynthesis, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes ppGpp from GTP, the pathway ppGpp biosynthesis and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi53Manganese1
    Metal bindingi77Manganese1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei81Nucleophile, for hydrolase activitySequence analysis1
    Active sitei82Nucleophile, for hydrolase activitySequence analysis1
    Metal bindingi144Manganese1
    Metal bindingi264MagnesiumSequence analysis1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Kinase, Transferase
    LigandATP-binding, GTP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q54089

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00908;UER00884

    UPA00908;UER00886

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:relA
    Synonyms:rel
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiStreptococcus dysgalactiae subsp. equisimilis (Streptococcus equisimilis)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri119602 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi44R → Q: No hydrolase activity. 1 Publication1
    Mutagenesisi78D → A: No hydrolase activity. 1 Publication1
    Mutagenesisi81E → G: No hydrolase activity. 1 Publication1
    Mutagenesisi82D → V: No hydrolase activity. 1 Publication1
    Mutagenesisi151T → A or P: No hydrolase activity. 1 Publication1
    Mutagenesisi264D → G: No synthase activity. 1 Publication1
    Mutagenesisi323E → Q: No synthase activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1163118

    Drug and drug target database

    More...
    DrugBanki
    DB02836 Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate
    DB04315 Guanosine-5'-Diphosphate

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001665651 – 739Bifunctional (p)ppGpp synthase/hydrolase RelAAdd BLAST739

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1739
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q54089

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q54089

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q54089

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini50 – 149HDPROSITE-ProRule annotationAdd BLAST100
    Domaini664 – 739ACTPROSITE-ProRule annotationAdd BLAST76

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the RelA/SpoT family.Curated

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00077 HDc, 1 hit
    cd05399 NT_Rel-Spo_like, 1 hit
    cd01668 TGS_RelA_SpoT, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.20.30, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002912 ACT_dom
    IPR012675 Beta-grasp_dom_sf
    IPR003607 HD/PDEase_dom
    IPR004811 RelA/Spo_fam
    IPR007685 RelA_SpoT
    IPR004095 TGS
    IPR012676 TGS-like
    IPR033655 TGS_RelA

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF13291 ACT_4, 1 hit
    PF13328 HD_4, 1 hit
    PF04607 RelA_SpoT, 1 hit
    PF02824 TGS, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00471 HDc, 1 hit
    SM00954 RelA_SpoT, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF81271 SSF81271, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00691 spoT_relA, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51671 ACT, 1 hit
    PS51831 HD, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q54089-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAKEINLTGE EVVALAAKYM NETDAAFVKK ALDYATAAHF YQVRKSGEPY
    60 70 80 90 100
    IVHPIQVAGI LADLHLDAVT VACGFLHDVV EDTDITLDNI EFDFGKDVRD
    110 120 130 140 150
    IVDGVTKLGK VEYKSHEEQL AENHRKMLMA MSKDIRVILV KLADRLHNMR
    160 170 180 190 200
    TLKHLRKDKQ ERISRETMEI YAPLAHRLGI SRIKWELEDL AFRYLNETEF
    210 220 230 240 250
    YKISHMMNEK RREREALVDD IVTKIKSYTT EQGLFGDVYG RPKHIYSIYR
    260 270 280 290 300
    KMRDKKKRFD QIFDLIAIRC VMETQSDVYA MVGYIHELWR PMPGRFKDYI
    310 320 330 340 350
    AAPKANGYQS IHTTVYGPKG PIEIQIRTKE MHQVAEYGVA AHWAYKKGVR
    360 370 380 390 400
    GKVNQAEQKV GMNWIKELVE LQDASNGDAV DFVDSVKEDI FSERIYVFTP
    410 420 430 440 450
    TGAVQELPKD SGPIDFAYAI HTQVGEKAIG AKVNGRMVPL TAKLKTGDVV
    460 470 480 490 500
    EIVTNPNSFG PSRDWIKLVK TNKARNKIRQ FFKNQDKELS VNKGRDMLVS
    510 520 530 540 550
    YFQEQGYVAN KYLDKKRIEA ILPKVSVKSE ESLYAAVGFG DISPVSVFNK
    560 570 580 590 600
    LTEKERREEE RAKAKAEAEE LVNGGEIKHE NKDVLKVRSE NGVIIQGASG
    610 620 630 640 650
    LLMRIAKCCN PVPGDPIEGY ITKGRGIAIH RADCNNIKSQ DGYQERLIEV
    660 670 680 690 700
    EWDLDNSSKD YQAEIDIYGL NRRGLLNDVL QILSNSTKSI STVNAQPTKD
    710 720 730
    MKFANIHVSF GIPNLTHLTT VVEKIKAVPD VYSVKRTNG
    Length:739
    Mass (Da):83,913
    Last modified:November 1, 1997 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE65CBEF99103D171
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X72832 Genomic DNA Translation: CAA51353.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S39975

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X72832 Genomic DNA Translation: CAA51353.1
    PIRiS39975

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VJ7X-ray2.10A/B1-385[»]
    ProteinModelPortaliQ54089
    SMRiQ54089
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    ChEMBLiCHEMBL1163118
    DrugBankiDB02836 Guanosine 5'-Diphosphate 2':3'-Cyclic Monophosphate
    DB04315 Guanosine-5'-Diphosphate

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayi
    UPA00908;UER00884

    UPA00908;UER00886

    SABIO-RKiQ54089

    Miscellaneous databases

    EvolutionaryTraceiQ54089

    Family and domain databases

    CDDicd00077 HDc, 1 hit
    cd05399 NT_Rel-Spo_like, 1 hit
    cd01668 TGS_RelA_SpoT, 1 hit
    Gene3Di3.10.20.30, 1 hit
    InterProiView protein in InterPro
    IPR002912 ACT_dom
    IPR012675 Beta-grasp_dom_sf
    IPR003607 HD/PDEase_dom
    IPR004811 RelA/Spo_fam
    IPR007685 RelA_SpoT
    IPR004095 TGS
    IPR012676 TGS-like
    IPR033655 TGS_RelA
    PfamiView protein in Pfam
    PF13291 ACT_4, 1 hit
    PF13328 HD_4, 1 hit
    PF04607 RelA_SpoT, 1 hit
    PF02824 TGS, 1 hit
    SMARTiView protein in SMART
    SM00471 HDc, 1 hit
    SM00954 RelA_SpoT, 1 hit
    SUPFAMiSSF81271 SSF81271, 1 hit
    TIGRFAMsiTIGR00691 spoT_relA, 1 hit
    PROSITEiView protein in PROSITE
    PS51671 ACT, 1 hit
    PS51831 HD, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRELA_STREQ
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q54089
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: December 5, 2018
    This is version 108 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

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