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Protein

Hemolysin expression-modulating protein Hha

Gene

hha

Organism
Escherichia coli (strain K12)
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

Down-regulates hemolysin (hly) expression in complex with H-NS (PubMed:1956303, PubMed:10778755, PubMed:11790731, PubMed:21600204). Stimulates transposition events in vivo (PubMed:8145648). Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex (PubMed:23543115). Binds DNA and influences DNA topology in response to environmental stimuli; does not however interact with DNA in the absence of H-NS (PubMed:23543115). Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR (PubMed:19909729). Decreases biofilm formation by repressing the transcription of fimbrial genes fimA and ihfA, and by repressing the transcription of tRNAs corresponding to rare codons, which are abundant in type 1 fimbrial genes (PubMed:18545668).9 Publications

Miscellaneous

Hha and TomB may form a type II toxin-antitoxin (TA) system (PubMed:18545668).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei25Interacts with H-NS1
Sitei48Interacts with H-NS1

<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 - Biological processi

  • regulation of gene expression Source: EcoCyc

<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 functionRepressor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10439-MONOMER

<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:
Hemolysin expression-modulating protein Hha
<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:hha
Ordered Locus Names:b0460, JW0449
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10439 hha

<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

  • cytosol Source: EcoCyc

<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 in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Deletion results in a large increase in the production of extracellular and intracellular hemolysin (PubMed:1956303). At low osmolarity minor changes in overall translation, at 0.4 M NaCl expression of about 25 proteins altered, including decreased OmpA, crr and AhpC (in strain 5K, not a K12 derivative) (PubMed:10322001). At 0.3 M NaCl in strain W3110 up-regulation of 113 genes and down-regulation of 8 genes was observed; a double cnu-hha deletion up-regulated 134 and down-regulated 5 genes, most of which are thought to have been acquired horizontally and are also up-regulated in double hns-stpA deletions (PubMed:23543115). However there are only 12 genes that were commonly up-regulated in the hha and cnu-hha deletions (PubMed:23543115). Represses the production of persister cells (PubMed:19909729). Deletion of hha and tomB (ybaJ), in the presence of a conjugative plasmid (R1drd19), decreases biofilm formation, cell aggregation and increases motility via flagella and motility gene expression (PubMed:16317765).5 Publications

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>Mutagenesisi10D → N: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi16R → C: Derepression of the hly operon, impaired H-NS binding. 1 Publication1
Mutagenesisi22D → N: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi25E → Q: Affects H-NS binding ability. Decrease in the ability to repress the expression of the hly operon. 1 Publication1
Mutagenesisi29E → Q: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi34E → Q: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi37D → N: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi39E → Q: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi44 – 72Missing : Derepression of the hly operon, impaired H-NS binding. 1 PublicationAdd BLAST29
Mutagenesisi48D → E or R: Abolishes the interaction with H-NS. 1 Publication1
Mutagenesisi48D → N: Abolishes the interaction with H-NS. Loss of the ability to repress the expression of the hly operon. 1 Publication1
Mutagenesisi50R → H: Derepression of the hly operon, impaired H-NS binding. 1 Publication1
Mutagenesisi58 – 72Missing : Derepression of the hly operon, impaired H-NS binding. 1 PublicationAdd BLAST15
Mutagenesisi61D → N: Does not affect H-NS binding ability. 1 Publication1
Mutagenesisi64P → L or S: Derepression of the hly operon, impaired H-NS binding. 1 Publication1
Mutagenesisi72R → RHHHHHH: Derepression of the hly operon, impaired H-NS binding. 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002017271 – 72Hemolysin expression-modulating protein HhaAdd BLAST72

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0ACE3

PRoteomics IDEntifications database

More...
PRIDEi
P0ACE3

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is autoregulated (Probable). Induced during biofilm formation (PubMed:14727089, PubMed:18545668).Curated2 Publications

<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

Forms a heterotrimeric complex with the H-NS dimer in the absence of DNA.5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
hnsP0ACF85EBI-1122578,EBI-544934

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262034, 9 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1979 H-NS-Hha transcription factor complex

Database of interacting proteins

More...
DIPi
DIP-9897N

Protein interaction database and analysis system

More...
IntActi
P0ACE3, 2 interactors

Molecular INTeraction database

More...
MINTi
P0ACE3

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0416

<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

172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0ACE3

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

More...
SMRi
P0ACE3

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P0ACE3

<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

<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

Histidine-tagging (His-tagging) at the N-terminus does not impair interaction with H-NS, whereas His-tagging at the C-terminus does impair interaction (PubMed:11790731).1 Publication

<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 Hha/YmoA/Cnu family.2 Publications

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105KF5 Bacteria
ENOG4111U15 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000219358

KEGG Orthology (KO)

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KOi
K05839

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1280.40, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007985 Hemolysn_expr_modulating_HHA
IPR036666 HHA_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05321 HHA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF68989 SSF68989, 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.

P0ACE3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEKPLTKTD YLMRLRRCQT IDTLERVIEK NKYELSDNEL AVFYSAADHR
60 70
LAELTMNKLY DKIPSSVWKF IR
Length:72
Mass (Da):8,628
Last modified:November 22, 2005 - 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:iA77211B87CF0134A
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB40215 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X57977 Genomic DNA Translation: CAA41043.1
U82664 Genomic DNA Translation: AAB40215.1 Different initiation.
U00096 Genomic DNA Translation: AAC73562.1
AP009048 Genomic DNA Translation: BAE76239.1

Protein sequence database of the Protein Information Resource

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PIRi
C64776

NCBI Reference Sequences

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RefSeqi
NP_414993.1, NC_000913.3
WP_001291435.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73562; AAC73562; b0460
BAE76239; BAE76239; BAE76239

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945098

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0449
eco:b0460

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.478

<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
X57977 Genomic DNA Translation: CAA41043.1
U82664 Genomic DNA Translation: AAB40215.1 Different initiation.
U00096 Genomic DNA Translation: AAC73562.1
AP009048 Genomic DNA Translation: BAE76239.1
PIRiC64776
RefSeqiNP_414993.1, NC_000913.3
WP_001291435.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JW2NMR-A1-72[»]
2MW2NMR-A1-72[»]
ProteinModelPortaliP0ACE3
SMRiP0ACE3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262034, 9 interactors
ComplexPortaliCPX-1979 H-NS-Hha transcription factor complex
DIPiDIP-9897N
IntActiP0ACE3, 2 interactors
MINTiP0ACE3
STRINGi316385.ECDH10B_0416

Proteomic databases

PaxDbiP0ACE3
PRIDEiP0ACE3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73562; AAC73562; b0460
BAE76239; BAE76239; BAE76239
GeneIDi945098
KEGGiecj:JW0449
eco:b0460
PATRICifig|511145.12.peg.478

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0434
EcoGeneiEG10439 hha

Phylogenomic databases

eggNOGiENOG4105KF5 Bacteria
ENOG4111U15 LUCA
HOGENOMiHOG000219358
KOiK05839

Enzyme and pathway databases

BioCyciEcoCyc:EG10439-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0ACE3

Protein Ontology

More...
PROi
PR:P0ACE3

Family and domain databases

Gene3Di1.20.1280.40, 1 hit
InterProiView protein in InterPro
IPR007985 Hemolysn_expr_modulating_HHA
IPR036666 HHA_sf
PfamiView protein in Pfam
PF05321 HHA, 1 hit
SUPFAMiSSF68989 SSF68989, 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 nameiHHA_ECOLI
<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: P0ACE3
Secondary accession number(s): P23870, P77120, Q2MBW7
<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 22, 2005
Last sequence update: November 22, 2005
Last modified: November 7, 2018
This is version 98 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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