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Entry version 139 (10 Apr 2019)
Sequence version 1 (01 Nov 1999)
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Protein

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase

Gene

murE

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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

Catalyzes the addition of both L- and D-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use meso-diaminopimelate as the amino acid substrate in vitro, although much less efficiently.1 Publication

Miscellaneous

The peptidoglycan of T.maritima was shown to contain approximate amounts of both enantiomers of lysine and no diaminopimelate.

<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 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

The catalytic efficiency for the L-lysine adding activity is 4-fold and 10-fold higher than that for the D-lysine and meso-diaminopimelate adding activity, respectively.
  1. KM=0.45 mM for UDP-N-acetylmuramoyl-L-Ala-D-Glu1 Publication
  2. KM=2.8 mM for L-lysine (at pH 9.4)1 Publication
  3. KM=0.65 mM for L-lysine (at pH 8)1 Publication
  4. KM=1.7 mM for D-lysine (at pH 9.4)1 Publication
  5. KM=1.0 mM for D-lysine (at pH 8)1 Publication
  6. KM=4.8 mM for meso-diaminopimelate (at pH 9.4)1 Publication
  7. KM=27 mM for L-ornithine (at pH 9.4)1 Publication
  8. KM=3.6 mM for ATP1 Publication

    pH dependencei

    Optimum pH is 9.4 for the L-lysine adding activity.1 Publication

    Temperature dependencei

    Optimum temperature is 68 degrees Celsius for the L-lysine adding activity.1 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: peptidoglycan biosynthesis

    This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
    View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei32UDP-MurNAc-L-Ala-D-GluBy similarity1
    Binding sitei179UDP-MurNAc-L-Ala-D-GluBy similarity1
    Binding sitei185UDP-MurNAc-L-Ala-D-GluBy similarity1
    Binding sitei187UDP-MurNAc-L-Ala-D-GluBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi110 – 116ATPSequence analysis7

    <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 functionLigase
    Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-16146

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

    More...
    UniPathwayi
    UPA00219

    <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:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase (EC:6.3.2.371 Publication, EC:6.3.2.71 Publication)
    Alternative name(s):
    D-lysine-adding enzyme
    L-lysine-adding enzyme
    UDP-MurNAc-L-Ala-D-Glu:LD-Lys ligase
    UDP-MurNAc-tripeptide synthetase
    UDP-N-acetylmuramyl-tripeptide synthetase
    <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:murE
    Ordered Locus Names:TM_0237
    <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>OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    <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 identifieri243274 [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 lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000008183 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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_00001019621 – 490UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligaseAdd BLAST490

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei219N6-carboxylysineBy similarity1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.By similarity

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9WY79

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    243274.THEMA_03540

    <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

    1490
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    4BUBX-ray2.90A/B1-490[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9WY79

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

    More...
    SMRi
    Q9WY79

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni152 – 153UDP-MurNAc-L-Ala-D-Glu bindingBy similarity2

    <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 MurCDEF family. MurE subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4107EEN Bacteria
    COG0769 LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9WY79

    KEGG Orthology (KO)

    More...
    KOi
    K01928

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    PKFRMSL

    Database of Orthologous Groups

    More...
    OrthoDBi
    1861122at2

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.1190.10, 1 hit
    3.90.190.20, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00208 MurE, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR018109 Folylpolyglutamate_synth_CS
    IPR036565 Mur-like_cat_sf
    IPR004101 Mur_ligase_C
    IPR036615 Mur_ligase_C_dom_sf
    IPR013221 Mur_ligase_cen
    IPR000713 Mur_ligase_N
    IPR035911 MurE/MurF_N
    IPR005761 UDP-N-AcMur-Glu-dNH2Pim_ligase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01225 Mur_ligase, 1 hit
    PF02875 Mur_ligase_C, 1 hit
    PF08245 Mur_ligase_M, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53244 SSF53244, 1 hit
    SSF53623 SSF53623, 1 hit
    SSF63418 SSF63418, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01085 murE, 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.

    Q9WY79-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNISTIVSNL KDLILEVRAP YDLEITGVSN HSSKVKKGDL FICRRGEKFD
    60 70 80 90 100
    SHEIIPEVME KGAVAVVVER EIDLDFPYIQ VFDSRYFEAK VASLFFEDPW
    110 120 130 140 150
    KDVLTFGVTG TNGKTTTTMM IYHMLTSLGE RGSVLTTAVK RILGNSYYDD
    160 170 180 190 200
    ITTPDAITIL SAMKENREGG GKFFALEVSS HALVQQRVEG VRFDVGIFTN
    210 220 230 240 250
    ISRDHLDFHG TFENYLKAKL HLFDLLKDDG VAVLNESLAD AFNRKSRKIT
    260 270 280 290 300
    FGTSKNADYR LGNIEVSWEG TQFVLETPDG LLKVFTRAIG DFNAYNAAAA
    310 320 330 340 350
    IAALHQLGYD PKDLASSLET FTGVEGRFEV VRGAKKIGLN VVVDFAHSPD
    360 370 380 390 400
    ALEKLLKNVR KISQGRVIVV FGAGGNSDRG KRPMMSEVAS KLADVVILTT
    410 420 430 440 450
    DDPRGEDPEQ IMEDLIKGID KRKPYLVLFD RREAIETALT IANRGDSVVI
    460 470 480 490
    AGRGHERYQI IDEEKKVPFQ DREVVEEIIR DKLKGRKYAQ
    Length:490
    Mass (Da):54,740
    Last modified:November 1, 1999 - 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:i21A6FBE388D741A9
    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
    AE000512 Genomic DNA Translation: AAD35328.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    G72402

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_228051.1, NC_000853.1
    WP_004082936.1, NZ_CP011107.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAD35328; AAD35328; TM_0237

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    897137

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    tma:TM0237

    <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
    AE000512 Genomic DNA Translation: AAD35328.1
    PIRiG72402
    RefSeqiNP_228051.1, NC_000853.1
    WP_004082936.1, NZ_CP011107.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4BUBX-ray2.90A/B1-490[»]
    ProteinModelPortaliQ9WY79
    SMRiQ9WY79
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243274.THEMA_03540

    Proteomic databases

    PRIDEiQ9WY79

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD35328; AAD35328; TM_0237
    GeneIDi897137
    KEGGitma:TM0237

    Phylogenomic databases

    eggNOGiENOG4107EEN Bacteria
    COG0769 LUCA
    InParanoidiQ9WY79
    KOiK01928
    OMAiPKFRMSL
    OrthoDBi1861122at2

    Enzyme and pathway databases

    UniPathwayi
    UPA00219

    BioCyciMetaCyc:MONOMER-16146

    Family and domain databases

    Gene3Di3.40.1190.10, 1 hit
    3.90.190.20, 1 hit
    HAMAPiMF_00208 MurE, 1 hit
    InterProiView protein in InterPro
    IPR018109 Folylpolyglutamate_synth_CS
    IPR036565 Mur-like_cat_sf
    IPR004101 Mur_ligase_C
    IPR036615 Mur_ligase_C_dom_sf
    IPR013221 Mur_ligase_cen
    IPR000713 Mur_ligase_N
    IPR035911 MurE/MurF_N
    IPR005761 UDP-N-AcMur-Glu-dNH2Pim_ligase
    PfamiView protein in Pfam
    PF01225 Mur_ligase, 1 hit
    PF02875 Mur_ligase_C, 1 hit
    PF08245 Mur_ligase_M, 1 hit
    SUPFAMiSSF53244 SSF53244, 1 hit
    SSF53623 SSF53623, 1 hit
    SSF63418 SSF63418, 1 hit
    TIGRFAMsiTIGR01085 murE, 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 nameiMURE_THEMA
    <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: Q9WY79
    <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: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: April 10, 2019
    This is version 139 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, Complete proteome, Reference proteome

    Documents

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