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Entry version 40 (13 Nov 2019)
Sequence version 2 (15 Feb 2017)
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Protein

N-acetyltransferase Eis

Gene

eis

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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

Effector that is released into the host cell and affects host immune responses; it negatively modulates inflammation, macrophage autophagy, and cell death through redox-dependent signaling (PubMed:17259625, PubMed:21187903). Acts as an acetyltransferase. Acetylates 'Lys-55' of dual-specificity protein phosphatase 16 (DUSP16)/mitogen-activated protein kinase phosphatase-7 (MKP-7), a JNK-specific phosphatase; this leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS (reactive oxygen species) generation for enhanced intracellular survival of M.tuberculosis (PubMed:22547814). Inhibits Con A-mediated T-cell proliferation in vitro (PubMed:17449476). Treatment of T-cells with Eis inhibits ERK1/2, JAK pathway, and subsequent production of tumor necrosis factor-alpha (TNF-alpha) and interleukin-4 (IL-4); on the contrary, there is increased production of interferon-gamma (IFN-gamma) and interleukin-10 (IL-10), which indicates that immunity in response to Eis treatment is skewed away from a protective T(H)1 response and Eis disturbs the cross regulation of T-cells (PubMed:17449476). When expressed in M.smegmatis, enhances intracellular survival of the bacteria in host macrophages during infection (PubMed:10629183).5 Publications
Can also acetylate multiple amine groups of many aminoglycoside (AG) antibiotics, leading to their inactivation, and thus contributes to drug resistance (PubMed:19906990, PubMed:21628583, PubMed:24106131). Is also able to acetylate and deactivate the cyclic peptide antibiotic capreomycin, but not the other anti-tuberculous drugs isoniazid and pyrazinamide (PubMed:23233486). Acetylates kanamycin (KAN) more efficiently than amikacin (AMK), even though Eis seems to bind AMK with higher affinity (PubMed:19906990). Does not acetylate and inactivate streptomycin, apramycin and spectinomycin (PubMed:19906990, PubMed:21628583).4 Publications

Miscellaneous

Increased expression of eis due to point mutations in the promoter region of eis is responsible for resistance to the second-line injectable drug kanamycin in a number of M.tuberculosis clinical isolates, through acetylation of its amino groups, which leads to inactivation of the drug.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

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

Is potently inhibited by several small-molecule that share an isothiazole S,S-dioxide heterocyclic core. Some of these inhibitors, when used in combination with KAN against resistant M.tuberculosis, efficiently overcome Eis-mediated KAN resistance by restoring the antibacterial activity of KAN.1 Publication

<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 0.020 sec(-1) with amikacin as substrate. kcat is 0.039 sec(-1) with kanamycin as substrate. kcat is 0.070 sec(-1) with neamine as substrate. kcat is 0.130 sec(-1) with neomycin B as substrate. kcat is 0.482 sec(-1) with netilmicin as substrate. kcat is 0.058 sec(-1) with paromomycin as substrate. kcat is 0.270 sec(-1) with sisomicin as substrate. kcat is 0.162 sec(-1) with tobramycin as substrate (at 25 degrees Celsius and pH 8.0) (PubMed:21628583). kcat is 0.017 sec(-1) with amikacin as substrate. kcat is 0.032 sec(-1) with kanamycin A as substrate. kcat is 0.032 sec(-1) with paromomycin as substrate. kcat is 0.179 sec(-1) with tobramycin as substrate (at 25 degrees Celsius and pH 8.0) (PubMed:22547814). kcat is 1.25 sec(-1) with capreomycin as substrate (at 25 degrees Celsius and pH 8.0) (PubMed:23233486). Catalytic efficiency is 3-fold higher for acetylation of kanamycin than for acetylation of amikacin (PubMed:19906990).3 Publications
  1. KM=112 µM for amikacin1 Publication
  2. KM=75 µM for amikacin (at 25 degrees Celsius and pH 8.0)1 Publication
  3. KM=73 µM for amikacin (at 25 degrees Celsius and pH 8.0)1 Publication
  4. KM=154 µM for kanamycin1 Publication
  5. KM=99 µM for kanamycin (at 25 degrees Celsius and pH 8.0)1 Publication
  6. KM=81 µM for kanamycin A (at 25 degrees Celsius and pH 8.0)1 Publication
  7. KM=178 µM for neamine (at 25 degrees Celsius and pH 8.0)1 Publication
  8. KM=98 µM for neomycin B (at 25 degrees Celsius and pH 8.0)1 Publication
  9. KM=48 µM for netilmicin (at 25 degrees Celsius and pH 8.0)1 Publication
  10. KM=82 µM for paromomycin (at 25 degrees Celsius and pH 8.0)1 Publication
  11. KM=85 µM for paromomycin (at 25 degrees Celsius and pH 8.0)1 Publication
  12. KM=58 µM for sisomicin (at 25 degrees Celsius and pH 8.0)1 Publication
  13. KM=63 µM for tobramycin (at 25 degrees Celsius and pH 8.0)1 Publication
  14. KM=71 µM for tobramycin (at 25 degrees Celsius and pH 8.0)1 Publication
  15. KM=654 µM for capreomycin (at 25 degrees Celsius and pH 8.0)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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei126Proton donor1 Publication1
    Active sitei402Proton acceptor; via carboxylate1 Publication1

    <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

    • aminoglycoside N-acetyltransferase activity Source: MTBBASE
    • identical protein binding Source: IntAct

    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 functionAcyltransferase, Transferase
    Biological processAntibiotic resistance

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MTBH37RV:G185E-6646-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:
    N-acetyltransferase EisCurated (EC:2.3.1.-3 Publications)
    Alternative name(s):
    Aminoglycoside N-acetyltransferase2 Publications
    Enhanced intracellular survival protein2 Publications
    Protein-lysine N-acetyltransferase1 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
    Name:eis1 Publication
    Ordered Locus Names:Rv2416c
    ORF Names:MTCY253.04
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <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
    • UP000001584 <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

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv2416c

    <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

    Host cytoplasmic vesicle, Secreted

    <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

    No significant difference in terms of intracellular survival in U-397 macrophages and in an in vivo mouse aerosol model of infection (PubMed:17259625). A strain lacking this gene induces more TNF-alpha but less IL-10 production in primary human monocytes than wild-type (PubMed:17259625). Macrophages infected with a M.tuberculosis eis-deletion mutant display markedly increased accumulation of massive autophagic vacuoles and formation of autophagosomes in vitro and in vivo (PubMed:21187903). Infection of macrophages with this mutant increases the production of tumor necrosis factor-alpha and interleukin-6 over the levels produced by infection with wild-type or complemented strains (PubMed:21187903). Elevated ROS generation in macrophages infected with this mutant (for which NADPH oxidase and mitochondria are largely responsible) render the cells highly sensitive to autophagy activation and cytokine production; despite considerable activation of autophagy and proinflammatory responses, these infected macrophages undergo caspase-independent cell death (PubMed:21187903).2 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>Mutagenesisi119H → A: Decreases catalytic activity on AG substrates, leads to a change in the number of acetylated sites. 1 Publication1
    Mutagenesisi126Y → A: Abolishes catalytic activity on AG substrates. 1 Publication1
    Mutagenesisi197W → A: Abolishes catalytic activity on AG substrates. 1 Publication1
    Mutagenesisi204C → A: No effect on catalytic activity on AG substrates. Prevents artifactual CoA adduct formation during crystallization. 1 Publication1
    Mutagenesisi292D → A: Nearly abolishes catalytic activity on AG substrates. 1 Publication1
    Mutagenesisi310Y → A: Nearly abolishes catalytic activity on AG substrates. 1 Publication1
    Mutagenesisi400 – 402Missing : Nearly abolishes catalytic activity on AG substrates. 1 Publication3

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3879870

    <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_processing_section">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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002202622 – 402N-acetyltransferase EisAdd BLAST401

    Proteomic databases

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

    More...
    PaxDbi
    P9WFK7

    <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

    Homohexamer; trimer of dimers.

    2 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
    itself2EBI-15929122,EBI-15929122

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv2416c

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P9WFK7

    <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

    1402
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    P9WFK7

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 154N-acetyltransferaseAdd BLAST152

    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>Regioni85 – 87Acetyl-CoA bindingCombined sources1 Publication1 Publication3
    Regioni93 – 98Acetyl-CoA bindingCombined sources3 Publications1 Publication6
    Regioni121 – 122Acetyl-CoA bindingCombined sources1 Publication1 Publication2

    <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

    The Eis monomer consists of three regions that are assembled into a heart-shaped molecule (PubMed:21628583). This shape is formed by an unusual fusion of two general control non-derepressible 5 (GCN5)-related N-acetyltransferase (GNAT) regions and a C-terminal region (PubMed:21628583). The N-acetyltransferase domain of Eis is responsible for its modulation of ROS generation and proinflammatory responses in macrophages (PubMed:21187903).2 Publications

    <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 acetyltransferase Eis family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105HHS Bacteria
    COG4552 LUCA

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1050.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01812 Eis, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR041380 Acetyltransf_17
    IPR016181 Acyl_CoA_acyltransferase
    IPR025559 Eis_dom
    IPR000182 GNAT_dom
    IPR022902 NAcTrfase_Eis
    IPR036527 SCP2_sterol-bd_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF17668 Acetyltransf_17, 1 hit
    PF13530 SCP2_2, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55718 SSF55718, 1 hit
    SSF55729 SSF55729, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51186 GNAT, 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.

    P9WFK7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTVTLCSPTE DDWPGMFLLA AASFTDFIGP ESATAWRTLV PTDGAVVVRD
    60 70 80 90 100
    GAGPGSEVVG MALYMDLRLT VPGEVVLPTA GLSFVAVAPT HRRRGLLRAM
    110 120 130 140 150
    CAELHRRIAD SGYPVAALHA SEGGIYGRFG YGPATTLHEL TVDRRFARFH
    160 170 180 190 200
    ADAPGGGLGG SSVRLVRPTE HRGEFEAIYE RWRQQVPGGL LRPQVLWDEL
    210 220 230 240 250
    LAECKAAPGG DRESFALLHP DGYALYRVDR TDLKLARVSE LRAVTADAHC
    260 270 280 290 300
    ALWRALIGLD SMERISIITH PQDPLPHLLT DTRLARTTWR QDGLWLRIMN
    310 320 330 340 350
    VPAALEARGY AHEVGEFSTV LEVSDGGRFA LKIGDGRARC TPTDAAAEIE
    360 370 380 390 400
    MDRDVLGSLY LGAHRASTLA AANRLRTKDS QLLRRLDAAF ASDVPVQTAF

    EF
    Length:402
    Mass (Da):43,804
    Last modified:February 15, 2017 - 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:iEF06F75C00F05333
    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 AAF03768 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    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
    AL123456 Genomic DNA Translation: CCP45207.1
    AF144099 Genomic DNA Translation: AAF03768.1 Different initiation.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    C70685

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_216932.2, NC_000962.3
    WP_003903886.1, NC_000962.3

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP45207; CCP45207; Rv2416c

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    885903

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv2416c
    mtv:RVBD_2416c

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|83332.12.peg.2706

    <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
    AL123456 Genomic DNA Translation: CCP45207.1
    AF144099 Genomic DNA Translation: AAF03768.1 Different initiation.
    PIRiC70685
    RefSeqiNP_216932.2, NC_000962.3
    WP_003903886.1, NC_000962.3

    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
    3R1KX-ray1.95A1-402[»]
    3RYOX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-402[»]
    3SXOX-ray2.50A/B1-402[»]
    3UY5X-ray2.50A1-402[»]
    4JD6X-ray3.50A/B/C/D/E/F1-402[»]
    5EBVX-ray2.20A2-402[»]
    5EC4X-ray2.21A2-402[»]
    5IV0X-ray2.10A1-402[»]
    5TVJX-ray2.30A2-402[»]
    6B0UX-ray2.80A/B/C1-402[»]
    6B3TX-ray2.40A1-402[»]
    6P3TX-ray2.50A1-402[»]
    6P3UX-ray2.55A1-402[»]
    6P3VX-ray2.50A1-402[»]
    SMRiP9WFK7
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2416c

    Chemistry databases

    BindingDBiP9WFK7
    ChEMBLiCHEMBL3879870

    Proteomic databases

    PaxDbiP9WFK7

    Genome annotation databases

    EnsemblBacteriaiCCP45207; CCP45207; Rv2416c
    GeneIDi885903
    KEGGimtu:Rv2416c
    mtv:RVBD_2416c
    PATRICifig|83332.12.peg.2706

    Organism-specific databases

    TubercuListiRv2416c

    Phylogenomic databases

    eggNOGiENOG4105HHS Bacteria
    COG4552 LUCA

    Enzyme and pathway databases

    BioCyciMTBH37RV:G185E-6646-MONOMER

    Family and domain databases

    Gene3Di3.30.1050.10, 1 hit
    HAMAPiMF_01812 Eis, 1 hit
    InterProiView protein in InterPro
    IPR041380 Acetyltransf_17
    IPR016181 Acyl_CoA_acyltransferase
    IPR025559 Eis_dom
    IPR000182 GNAT_dom
    IPR022902 NAcTrfase_Eis
    IPR036527 SCP2_sterol-bd_dom_sf
    PfamiView protein in Pfam
    PF17668 Acetyltransf_17, 1 hit
    PF13530 SCP2_2, 1 hit
    SUPFAMiSSF55718 SSF55718, 1 hit
    SSF55729 SSF55729, 1 hit
    PROSITEiView protein in PROSITE
    PS51186 GNAT, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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 nameiEIS_MYCTU
    <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: P9WFK7
    Secondary accession number(s): L0TCA0, P71727, Q9RG79
    <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: April 16, 2014
    Last sequence update: February 15, 2017
    Last modified: November 13, 2019
    This is version 40 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    UniProt is an ELIXIR core data resource
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