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Entry version 63 (02 Jun 2021)
Sequence version 1 (10 Jun 2008)
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Protein

Alginate lyase

Gene

Smlt2602

Organism
Stenotrophomonas maltophilia (strain K279a)
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

Polysaccharide lyase that catalyzes the depolymerization of alginate via a beta-elimination mechanism, cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues. Acts specifically on alginate and each of its block structures, with highest activity toward poly-beta-D-mannuronate (poly-ManA). Shows an exolytic mode of action, producing unsaturated monomers. Displays a very low activity against poly-beta-D-glucuronate (poly-GlcA), and is not active on poly-alpha-D-galacturonate, hyaluronan, heparin, heparan sulfate and chondroitin sulfate.

1 Publication

<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

  • Cleavage of 4-deoxy-alpha-L-erythro-hex-4-enopyranuronoside oligosaccharides into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides.1 Publication EC:4.2.2.26

<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

Zn2+By similarityNote: The zinc ion likely plays a structural role.By similarity

<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

kcat is 34.8 sec(-1) with alginate as substrate. kcat is 62.2 sec(-1) with poly-ManA as substrate. kcat is 34.6 sec(-1) with poly-GulA as substrate. kcat is 22.2 sec(-1) with poly-MG as substrate. kcat is 0.4 sec(-1) with poly-GlcA as substrate.1 Publication
  1. KM=0.67 mM for alginate1 Publication
  2. KM=0.41 mM for poly-ManA1 Publication
  3. KM=5.99 mM for poly-GulA1 Publication
  4. KM=0.57 mM for poly-MG1 Publication
  5. KM=1.40 mM for poly-GlcA1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei143SubstrateBy similarity1
Binding sitei204SubstrateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei207Neutralizes the sugar carboxylate group at subsite +11 Publication1
Binding sitei208SubstrateBy similarity1
Sitei208Neutralizes the sugar carboxylate group at subsite +11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei264Proton donor1 Publication1
Active sitei418Proton acceptor1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi420Zinc; via pros nitrogenBy similarity1
Metal bindingi438ZincBy similarity1
Binding sitei443SubstrateBy similarity1
Metal bindingi469Zinc; via tele nitrogenBy similarity1
Binding sitei669SubstrateBy similarity1

<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 functionLyase
Biological processCarbohydrate metabolism, Polysaccharide degradation
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
SMAL522373:SMLT_RS12410_1-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.2.26, 5134

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
B2FSW8

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
PL17, Polysaccharide Lyase Family 17

<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:
Alginate lyase1 Publication (EC:4.2.2.261 Publication)
Alternative name(s):
Exolytic alginate lyaseCurated
Exolytic polysaccharide lyase1 Publication
<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
Ordered Locus Names:Smlt2602Imported
<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>OrganismiStenotrophomonas maltophilia (strain K279a)
<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 identifieri522373 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
<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
  • UP000008840 <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

Keywords - Cellular componenti

Periplasm

<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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Is an attractive candidate for the broad-spectrum digestion of polyuronides into fermentable monomers for biofuel production.1 Publication

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>Mutagenesisi153Q → A or N: 2- to 3-fold decrease in activity against alginate and its three block structures. 1 Publication1
Mutagenesisi207N → L: Complete loss of activity against alginate and its three block structures. 1 Publication1
Mutagenesisi208H → A: Displays same catalytic activity toward poly-GlcA as wild-type. 1 Publication1
Mutagenesisi208H → F: Exhibits 30% of wild-type activity against alginate and poly-ManA and 5 and 8% wild-type activity against poly-GulA and poly-MG, respectively. Significantly influences the substrate specificity since the mutant exhibits significant exolytic activity toward poly-GlcA, with a 35-fold increase in catalytic efficiency over wild-type toward poly-GlcA, a non-alginate-based substrate. 1 Publication1
Mutagenesisi264Y → F: Complete loss of activity against alginate and its three block structures. 1 Publication1
Mutagenesisi418H → F: Complete loss of activity against alginate and its three block structures. 1 Publication1
Mutagenesisi455Y → F: Displays less than 1% alginate and poly-ManA activity compared to wild-type, yet approximately 8 and 4% wild-type activity toward poly-GulA and poly-MG. 1 Publication1

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 26Sequence analysisAdd BLAST26
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500277761827 – 742Alginate lyaseAdd BLAST716

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
B2FSW8

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
522373.Smlt2602

<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

3D structure databases

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

More...
SMRi
B2FSW8

Database of comparative protein structure models

More...
ModBasei
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>Regioni153 – 156Substrate bindingBy similarity4
Regioni263 – 266Substrate bindingBy similarity4

<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 polysaccharide lyase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502Z7XC, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_022650_0_0_6

Identification of Orthologs from Complete Genome Data

More...
OMAi
EGPYYQR

Database of Orthologous Groups

More...
OrthoDBi
442785at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.100, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008397, Alginate_lyase_dom
IPR008929, Chondroitin_lyas
IPR012480, Hepar_II_III

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05426, Alginate_lyase, 1 hit
PF07940, Hepar_II_III, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48230, SSF48230, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

B2FSW8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRLQPLFVSL ALAAPCALLP TASLSAAPAA AARQADTAPV LVTAAQWQQM
60 70 80 90 100
ASEGRRYPWF AKEQARTEAT LKKMMKAGID VPVPRDKGGG RTHEQHKRNY
110 120 130 140 150
QALLAAGTLY RLTGDRAYVD YARDMLLQYA QLYPTLGPHP EGRGQIPGRV
160 170 180 190 200
FWQVLNDSVW LVNAIQGYDA IRDALSAEDR NTIESKVFRP MAEFLVSEPK
210 220 230 240 250
NYDQIHNHAT WAVAATGMTG YVLRDQELVE KSLRGSQKDD KFGFLRQIDL
260 270 280 290 300
LFSPDGYYEE GPYYQRYALA PFLLFANAIE RNEPQRKIFA RRDGVLLKAV
310 320 330 340 350
DVLVQSSYGG LFFPINDAIL DKGIDTEELV AGIGIAYART GDDRLLSVAE
360 370 380 390 400
QQKRLLLSPE GLQVAQALAA NKAKPFDYHP MLLRDGPDGD RGGLAILRMN
410 420 430 440 450
GERGQALVQK DTMQGMGHGH FDKLNWLFYD NGNPVVTDYG AARFLNVEAK
460 470 480 490 500
RGGIYLAENR SWAKQTVAHN TLVVDEQSHF NGNWKRGEAH APQVRFFQAD
510 520 530 540 550
ADTQIASATM RDAYPGVAFT RTQALLRHPD LGLPVVLDLL QVHGDKAARY
560 570 580 590 600
DLPLHFNGHI VTTGFEAEHF PSQRPVLGKD NGYQHLWLDA RSKPGSEPRS
610 620 630 640 650
LAWLLDGRFY TYRFGSSAPA QALLVESGAN DPEFNLRREP ALLQRVDGQK
660 670 680 690 700
DVTFFSVLEP HGEYNGTAEY VHGADSRIRE IVRTRGSDAE VIELRLASGA
710 720 730 740
RIALGVADNS ATTSEHSVTV DGHVYRWNGS HARLDRSKGD GK
Length:742
Mass (Da):82,406
Last modified:June 10, 2008 - 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:i2E560A37F5F0A57B
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
AM743169 Genomic DNA Translation: CAQ46078.1

NCBI Reference Sequences

More...
RefSeqi
WP_012480338.1, NC_010943.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAQ46078; CAQ46078; Smlt2602

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sml:Smlt2602

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|522373.3.peg.2443

<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
AM743169 Genomic DNA Translation: CAQ46078.1
RefSeqiWP_012480338.1, NC_010943.1

3D structure databases

SMRiB2FSW8
ModBaseiSearch...

Protein-protein interaction databases

STRINGi522373.Smlt2602

Protein family/group databases

CAZyiPL17, Polysaccharide Lyase Family 17

Proteomic databases

PRIDEiB2FSW8

Genome annotation databases

EnsemblBacteriaiCAQ46078; CAQ46078; Smlt2602
KEGGisml:Smlt2602
PATRICifig|522373.3.peg.2443

Phylogenomic databases

eggNOGiENOG502Z7XC, Bacteria
HOGENOMiCLU_022650_0_0_6
OMAiEGPYYQR
OrthoDBi442785at2

Enzyme and pathway databases

BioCyciSMAL522373:SMLT_RS12410_1-MONOMER
BRENDAi4.2.2.26, 5134
SABIO-RKiB2FSW8

Family and domain databases

Gene3Di1.50.10.100, 1 hit
InterProiView protein in InterPro
IPR008397, Alginate_lyase_dom
IPR008929, Chondroitin_lyas
IPR012480, Hepar_II_III
PfamiView protein in Pfam
PF05426, Alginate_lyase, 1 hit
PF07940, Hepar_II_III, 1 hit
SUPFAMiSSF48230, SSF48230, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiEALGL_STRMK
<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: B2FSW8
<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 11, 2016
Last sequence update: June 10, 2008
Last modified: June 2, 2021
This is version 63 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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