Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 131 (23 Feb 2022)
Sequence version 2 (24 Oct 2001)
Previous versions | rss
Add a publicationFeedback
Protein

Methylmalonyl-CoA mutase

Gene

bhbA

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
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

Radical enzyme that catalyzes the transformation of methylmalonyl-CoA to succinyl-CoA. Is required for growth on the polyhydroxyalkanoate degradation pathway intermediates 3-hydroxybutyrate and acetoacetate as sole carbon source.

2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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:

<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=0.11 mM for (R,S)-methylmalonyl-CoA (in the presence of 3 mM NH4+)1 Publication
  2. KM=0.13 mM for (R,S)-methylmalonyl-CoA (in the absence of 3 mM NH4+)1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: propanoyl-CoA degradation

This protein is involved in step 3 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.Curated This subpathway is part of the pathway propanoyl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei195SubstrateBy similarity1
Binding sitei222SubstrateBy similarity1
Binding sitei232SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi593Cobalt (cobalamin axial ligand)By 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

<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 functionIsomerase
LigandCobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00945;UER00910

<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%5Fand%5Ftaxonomy%5Fsection">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:
Methylmalonyl-CoA mutase2 Publications (EC:5.4.99.21 Publication1 Publication)
Short name:
MCM1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:bhbA1 Publication
Ordered Locus Names:RB1449
ORF Names:SMb20757
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pSymB (megaplasmid 2)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri266834 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaProteobacteriaAlphaproteobacteriaHyphomicrobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000001976 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Plasmid pSymB

<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

Cells lacking this gene show no methylmalonyl-CoA mutase activity, in contrast to wild-type.1 Publication

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00001942742 – 712Methylmalonyl-CoA mutaseAdd BLAST711

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
266834.SM_b20757

<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
O86028

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini580 – 712B12-bindingPROSITE-ProRule annotationAdd BLAST133

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>Regioni73 – 77Substrate bindingBy similarity5
Regioni183 – 185Substrate bindingBy similarity3
Regioni271 – 273Substrate bindingBy similarity3

<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 methylmalonyl-CoA mutase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1884, Bacteria
COG2185, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_009523_3_1_5

Identification of Orthologs from Complete Genome Data

More...
OMAi
IAQKEWV

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006159, Acid_CoA_mut_C
IPR016176, Cbl-dep_enz_cat
IPR006158, Cobalamin-bd
IPR036724, Cobalamin-bd_sf
IPR006099, MeMalonylCoA_mutase_a/b_cat
IPR006098, MMCoA_mutase_a_cat

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02310, B12-binding, 1 hit
PF01642, MM_CoA_mutase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51703, SSF51703, 1 hit
SSF52242, SSF52242, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00640, acid_CoA_mut_C, 1 hit
TIGR00641, acid_CoA_mut_N, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51332, B12_BINDING, 1 hit
PS00544, METMALONYL_COA_MUTASE, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

O86028-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTEKTIKDWE ALAEKELRVS PEGLVWHTPE GIDVKPLYTS DDMSGIGHLN
60 70 80 90 100
SLPGFEPFVR GPRATMYAGR PWTVRQYAGF STAEASNAFY RRNLAAGQQG
110 120 130 140 150
VSVAFDLATH RGYDSDHPRV QGDVGKAGVA IDSVEDMKIL FDGIPLDRIS
160 170 180 190 200
VSMTMNGAVI PILASFIVAG EEQGVSRDKL SGTIQNDILK EFMVRNTYIY
210 220 230 240 250
PPEPSMRIVA DIIEYTAKEM PKFNSISISG YHMQEAGATL VQELAFTLAD
260 270 280 290 300
GREYVRAALA KGLNVDDFAG RLSFFFAIGM NFFMEAAKLR AARLLWTRIM
310 320 330 340 350
QEFKPEKASS LMLRTHCQTS GVSLQEQDPY NNIVRTAFEA MSAVLGGTQS
360 370 380 390 400
LHTNSFDEAM ALPTDFSARI ARNTQLILQH ETGVTKVVDP LAGSYYVESL
410 420 430 440 450
TNELAEKAWG LIEEVEALGG MTKAVNAGLP KRLIEEAATR RQAAVDRAEE
460 470 480 490 500
VIVGVNKYRL ENEQPIDILQ IDNAAVRTAQ VKRIEETRRR RDSQKMKQAL
510 520 530 540 550
DALADVARSG KGNLLAAAVE AARARATVGE ITDAMREAFG DYTAIPEVVT
560 570 580 590 600
DIYGKAYEGD PELGVLAGRL GEATKRLGHK PKIMVAKLGQ DGHDRGAKVI
610 620 630 640 650
ASAFGDIGFD VVAGPLFQTP EEAADLALAE EVTVIGVSSL AAGHRTLMPQ
660 670 680 690 700
LAEALKKRGG EDIIVVCGGV IPRQDYDYLM ENGVAAVFGP GTQVLDAARA
710
VLDLIEGKRR NV
Length:712
Mass (Da):77,501
Last modified:October 24, 2001 - v2
<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:i44FFD1D30294C5E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti47G → R in AAD13665 (PubMed:9889346).Curated1
Sequence conflicti61G → R in AAD13665 (PubMed:9889346).Curated1
Sequence conflicti156N → K in AAD13665 (PubMed:9889346).Curated1

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
AF080073 Genomic DNA Translation: AAD13665.1
AL591985 Genomic DNA Translation: CAC49849.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A96023

NCBI Reference Sequences

More...
RefSeqi
NP_437989.1, NC_003078.1
WP_010976251.1, NC_003078.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAC49849; CAC49849; SM_b20757

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
61601358

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sme:SM_b20757

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|266834.11.peg.6375

<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
AF080073 Genomic DNA Translation: AAD13665.1
AL591985 Genomic DNA Translation: CAC49849.1
PIRiA96023
RefSeqiNP_437989.1, NC_003078.1
WP_010976251.1, NC_003078.1

3D structure databases

SMRiO86028
ModBaseiSearch...

Protein-protein interaction databases

STRINGi266834.SM_b20757

Genome annotation databases

EnsemblBacteriaiCAC49849; CAC49849; SM_b20757
GeneIDi61601358
KEGGisme:SM_b20757
PATRICifig|266834.11.peg.6375

Phylogenomic databases

eggNOGiCOG1884, Bacteria
COG2185, Bacteria
HOGENOMiCLU_009523_3_1_5
OMAiIAQKEWV

Enzyme and pathway databases

UniPathwayiUPA00945;UER00910

Family and domain databases

InterProiView protein in InterPro
IPR006159, Acid_CoA_mut_C
IPR016176, Cbl-dep_enz_cat
IPR006158, Cobalamin-bd
IPR036724, Cobalamin-bd_sf
IPR006099, MeMalonylCoA_mutase_a/b_cat
IPR006098, MMCoA_mutase_a_cat
PfamiView protein in Pfam
PF02310, B12-binding, 1 hit
PF01642, MM_CoA_mutase, 1 hit
SUPFAMiSSF51703, SSF51703, 1 hit
SSF52242, SSF52242, 1 hit
TIGRFAMsiTIGR00640, acid_CoA_mut_C, 1 hit
TIGR00641, acid_CoA_mut_N, 1 hit
PROSITEiView protein in PROSITE
PS51332, B12_BINDING, 1 hit
PS00544, METMALONYL_COA_MUTASE, 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 nameiMCM_RHIME
<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: O86028
<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%5Fand%5Fisoforms">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: October 24, 2001
Last modified: February 23, 2022
This is version 131 of the entry and version 2 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

Direct protein sequencing, Plasmid, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again