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 34 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

6 kDa early secretory antigenic target

Gene

esxA

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

A secreted protein that plays a number of roles in modulating the host's immune response to infection as well as being responsible for bacterial escape into the host cytoplasm. Acts as a strong host (human) T-cell antigen (PubMed:7729876, PubMed:11940590). Inhibits IL-12 p40 (IL12B) and TNF-alpha expression by infected host (mouse) macrophages, reduces the nitric oxide response by about 75% (PubMed:14557536). In mice previously exposed to the bacterium, elicits high level of IFN-gamma production by T-cells upon subsequent challenge by M.tuberculosis, in the first phase of a protective immune response (PubMed:7897219, PubMed:7729876). Higher levels (1.6-3.3 µM) of recombinant protein inhibit IFN-gamma production by host (human) T-cells and also IL-17 and TNF-alpha production but not IL-2; decreases expression of host ATF-2 and JUN transcription factors by affecting T-cell receptors signaling downstream of ZAP70, without cytotoxicity or apoptosis (PubMed:19265145). EsxA inhibits IFN-gamma production in human T-cells by activating p38 MAPK (MAPK14), p38 MAPK is not responsible for IL-17 decrease (PubMed:21586573). Binds host (mouse) Toll-like receptor 2 (TLR2) and decreases host MYD88-dependent signaling; binding to TLR2 activates host kinase AKT and subsequently inhibits downstream activation of NF-kappa-B; the C-terminal 20 residues (76-95) are necessary and sufficient for the TLR2 inhibitory effect (PubMed:17486091). Required for induction of host (human) IL-1B maturation and release by activating the host NLRP3/ASC inflammasome; may also promote access of other tuberculosis proteins to the host cells cytoplasm (PubMed:20148899). Induces IL-8 (CXCL8) expression in host (human) lung epithelial cells (PubMed:23867456). Exogenously applied protein, or protein expressed in host (human and mouse), binds beta-2-microglobulin (B2M) and decreases its export to the cell surface, probably leading to defects in class I antigen presentation by the host cell (PubMed:25356553). Responsible for mitochondrial fragmention, redistribution around the cell nucleus and decreased mitochondrial mass; this effect is not seen until 48 hours post-infection (PubMed:26092385). Able to disrupt artificial planar bilayers in the absence of EsxB (CFP-10) (PubMed:14557547). Native protein binds artificial liposomes in the absence but not presence of EsxB and is able to rigidify and lyse them; the EsxA-EsxB complex dissociates at acidic pH, EsxB might serve as a chaperone to prevent membrane lysis (PubMed:17557817). Recombinant protein induces leakage of phosphocholine liposomes at acidic pH in the absence of ExsB, undergoes conformational change, becoming more alpha-helical at acidic pH (PubMed:23150662, PubMed:25645924). The study using recombinant protein did not find dissociation of EsxA-EsxB complex at acidic pH (PubMed:23150662). Involved in translocation of bacteria from the host (human) phagolysosome to the host cytoplasm (PubMed:17604718, PubMed:22319448). Translocation into host cytoplasm is visible 3 days post-infection using cultured human cells and precedes host cell death (PubMed:22319448). Recombinant protein induces apoptosis in host (human) differentiated cell lines, which is cell-line dependent; bacteria missing the ESX-1 locus do not induce apoptosis (PubMed:17298391). Host (human) cells treated with EsxA become permeable to extracellular dye (PubMed:17298391). EsxA and EsxA-EsxB are cytotoxic to pneumocytes (PubMed:19906174). ESX-1 secretion system-induced host (mouse) cell apoptosis, which is probably responsible for infection of new host cells, might be due to EsxA (PubMed:23848406). EsxA induces necrosis in aged neutrophils (PubMed:25321481). May help regulate assembly and function of the type VII secretion system (T7SS) (By similarity). EsxA disassembles pre-formed EccC-EsxB multimers, possibly by making EccC-EsxA-EsxB trimers instead of EccC-EsxB-EsxB-EccC tetramers (By similarity).By similarity1 Publication19 Publications
May be critical in pro-bacteria versus pro-host interactions; ESX-1 mediates DNA mediated export (maybe via EsxA). The DNA interacts with host (human) cGAS, leading to cGAMP production and activation of the host STING-TBK-1-IRF-3 signaling pathway that leads to IFN-beta which is thought to be 'pro-bacteria'. Mycobacterial dsDNA also interacts with AIM2-NLRP3-ASC to activate an inflammasome, leading to the 'pro-host' IL-1-beta (PubMed:26048138, PubMed:26048136).2 Publications

Miscellaneous

Genes esxA and esxB are part of RD1 (part of a 15-gene locus known as ESX-1), a section of DNA deleted in the M.bovis BCG strain used for vaccination. Deletion of this region is thought to be largely responsible for the attenuation of BCG, and esxA and esxB in particular are very important in this effect (PubMed:14557547, PubMed:14756778, PubMed:16368961, PubMed:17298391, PubMed:22319448, PubMed:22524898).6 Publications
Secretion of EspA, EsxA and EsxB is mutually dependent (PubMed:16030141).1 Publication
To improve expression in E.coli the proteins were cloned as a single protein in the order esxB-esxA with a cleavable thrombin tag (PubMed:19854905).1 Publication
2 inhibitors of ESX-1 secretion decrease secretion of this protein, without being bacteriocidal. BTP15 inhibits autophosphorylation of MprB with subsequent up-regulation of espA and decreased secretion of EspB and EsxA. BBH7 also inhibits TAT-dependent secretion of (at least) Ag85C (fbpC) and up-regulates members of the ESX-5 locus as well as other genes that are involved in cell wall biogenesis and metal ion homeostasis (PubMed:25299337).1 Publication

<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

Biological processApoptosis, Virulence

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-8173-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:
6 kDa early secretory antigenic target1 Publication
Alternative name(s):
ESAT-6
<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:esxA1 Publication
Synonyms:esaT6
Ordered Locus Names:Rv3875
ORF Names:MTV027.10
<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
Rv3875

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei11 – 43Helical1 PublicationAdd BLAST33
Transmembranei49 – 85Helical1 PublicationAdd BLAST37

GO - Cellular componenti

Keywords - Cellular componenti

Cell wall, Host cell membrane, Host cytoplasm, Host endoplasmic reticulum, Host membrane, Membrane, 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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

A good candiate for vaccine development (PubMed:7897219). It has been tested in a number of experimental situations.1 Publication

<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

Bacteria no longer translocate from the phagolysosome to the cytosol of host (human) cells; bacteria replicate only in host phagolysosome rather than cytoplasm, decreased apoptosis of infected host (human) dendritic cells (PubMed:17604718). Bacteria missing the RD1 locus do not gain access to host (human) cytoplasm; complementation with the RD1 locus restores access, but if EsxA is missing the last 12 residues cytoplasmic access is not restored although truncated EsxA is secreted by bacteria (PubMed:22319448). Loss of ability to lyse host (human) lung epithelial cells, possibly due to polar effects from the upstream esxB gene; in BALB/c-infected mice bacteria are not as invasive and cause decreased lung disease (PubMed:14557547). No growth in the human macrophage-like cell line THP-1, no cytotoxicity (PubMed:14756778). Severely attenutated infection in mice, nearly 1000-fold less bacteria in lung and spleen of C57BL/6 (PubMed:14557536, PubMed:14756778). Inactivation leads to absence of EsxA and EsxB from cell lysates (PubMed:14756778, PubMed:16368961). No secretion of EspA (PubMed:16030141). No longer decreases expression of IL-12 p40 and TNF-alpha by infected murine macrophages, while the nitric oxide response is only partially reduced (PubMed:14557536). Significantly decreased production of IL-1 beta (IL1B), decreased activation of host (human) CASP-1 in response to bacterial infection (PubMed:20148899). Mitochondrial morphology is no longer perturbed in human alveolar epithelial cell line A549 (PubMed:26092385).9 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>Mutagenesisi2 – 10Missing : 40% reduction in liposome disruption. 80% reduction; when associated with 86-T--A-95. 1 Publication9
Mutagenesisi2T → H: Wild-type virulence in an esxA deletion strain; protein should not be acetylated. 1 Publication1
Mutagenesisi4Q → L: Wild-type virulence in an esxA deletion strain. 1 Publication1
Mutagenesisi8F → I: Wild-type virulence in an esxA deletion strain. 1 Publication1
Mutagenesisi14A → R: Wild-type virulence in an esxA deletion strain. 1 Publication1
Mutagenesisi17A → E: 88% reduction in liposome disruption; when associated with 25-T-A-26. 1 Publication1
Mutagenesisi21N → C: Cannot be overproduced and purified. 1 Publication1
Mutagenesisi25 – 26IH → TA: 40% reduction in liposome disruption. 88% reduction in liposome disruption; when associated with E-17. Reduced liposome disruption; when associated with T-38. 1 Publication2
Mutagenesisi26H → A: 16% reduction in liposome disruption. 1 Publication1
Mutagenesisi28 – 29LL → AS: Does not restore virulence in an esxA deletion strain, decreased secretion of EsxA and EsxB. 1 Publication2
Mutagenesisi34Q → C: NBD-linked protein does not fluoresce at acidic pH in presence of liposomes, this residue may face inwards in membranes away from lipids. 1 Publication1
Mutagenesisi35S → C: NBD-linked protein fluoresces at acidic pH in presence of liposomes, suggests this residue faces lipids. 1 Publication1
Mutagenesisi37T → C: NBD-linked protein does not fluoresce at acidic pH in presence of liposomes, this residue may face inwards in membranes away from lipids. 1 Publication1
Mutagenesisi38K → T: Reduced liposome disruption; when associated with 25-T-A-26. 1 Publication1
Mutagenesisi43W → R: Does not restore virulence in an esxA deletion strain, wild-type secretion of EsxA and EsxB but no complex formed (PubMed:16048998). No effect on host TLR2-signaling. 2 Publications1
Mutagenesisi45G → C: NBD-linked protein moderately fluoresces at acidic pH in presence of liposomes, suggests this residue is partially within membrane. 1 Publication1
Mutagenesisi45G → T: Does not restore virulence in an esxA deletion strain, wild-type secretion of EsxA and EsxB. 1 Publication1
Mutagenesisi55 – 56QQ → IA: Wild-type virulence in an esxA deletion strain. 1 Publication2
Mutagenesisi55Q → C: NBD-linked protein does not fluoresce at acidic pH in presence of liposomes, this residue may face inwards in membranes away from lipids. 1 Publication1
Mutagenesisi58W → C: Cannot be overproduced and purified. 1 Publication1
Mutagenesisi60A → C: NBD-linked protein fluoresces at acidic pH in presence of liposomes, suggests this residue faces lipids. 1 Publication1
Mutagenesisi66 – 67NN → IA: Wild-type virulence in an esxA deletion strain. 1 Publication2
Mutagenesisi67N → L: Reduced liposome disruption; when associated with 25-T-A-26. 1 Publication1
Mutagenesisi74R → Q: Reduced liposome disruption; when associated with 25-T-A-26. 1 Publication1
Mutagenesisi83M → I: Wild-type virulence in an esxA deletion strain. 1 Publication1
Mutagenesisi84 – 95Missing : Bacteria no longer gain access to host cytoplasm via phagosomal rupture. 2 PublicationsAdd BLAST12
Mutagenesisi86 – 95Missing : 40% reduction in liposome disruption. 80% reduction; when associated with 2-T--G-10. 1 Publication10
Mutagenesisi87E → K: Abolishes EsxB-EsxA heterodimer interaction with EccCb1, maintains interaction with EspA, EccA2 and EccE2. 1 Publication1
Mutagenesisi90 – 95Missing : No longer inhibits host TLR2-signaling (PubMed:17486091). Does not interact with host B2M, does not decrease B2M cell surface expression, no defects in antigen presentation (PubMed:25356553). 2 Publications6
Mutagenesisi90 – 94VTGMF → RTGTQ: No longer inhibits host TLR2-signaling. 1 Publication5
Mutagenesisi90V → R: Does not restore virulence in an esxA deletion strain, wild-type secretion of EsxA and EsxB (PubMed:16048998). Partially inhibits host TLR2-signaling (PubMed:17486091). 2 Publications1
Mutagenesisi93M → T: Partially restores virulence in an esxA deletion strain, wild-type secretion of EsxA and EsxB (PubMed:16048998). Partially inhibits host TLR2-signaling (PubMed:17486091). 2 Publications1
Mutagenesisi94F → Q: Does not restore virulence in an esxA deletion strain, wild-type secretion of EsxA and EsxB (PubMed:16048998). Partially inhibits host TLR2-signaling (PubMed:17486091). 2 Publications1

<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 methionineiRemovedCombined sources2 Publications
<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_00001677932 – 956 kDa early secretory antigenic targetAdd BLAST94

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylthreonine; partialCombined sources1 Publication1

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

Upon purification from strain ATCC 27294 a C-terminally truncated peptide (missing residues 85-95) has been found; it is not clear if this is physiologically relevant (PubMed:15378760). An additional unknown modification on peptide Thr-86-Ala-95 has also been seen (PubMed:15378760).1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
P9WNK7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P9WNK7

<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

Constitutively expressed in culture (at protein level) (PubMed:9846755, PubMed:23848406). Up-regulated in infected human pneumonocytes (PubMed:19906174). Zinc increases secreted levels of this protein; 0.5 mM Zn2+, the physiological concentration in macrophages, induces 6-fold more secreted protein (PubMed:25299337). Part of the esxB-esxA operon (PubMed:9846755).4 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 tight 1:1 complex with EsxB (CFP-10) (PubMed:11940590, PubMed:14557536, PubMed:16048998, PubMed:16973880, PubMed:19854905, PubMed:19906174, PubMed:23150662, PubMed:26260636, PubMed:20085764, PubMed:15973432, PubMed:24586681). The complex persists even after secretion (PubMed:16048998). Recombinant His-tagged protein forms dimers and higher order multimers; how the protein is prepared influences its multimerization and its subsequent properties in vitro (PubMed:26260636). In vitro EsxB only interacts with non-acetylated EsxA; it also interacts with C-terminally truncated EsxA (missing the last 10 residues) (PubMed:15378760). The native EsxA-EsxB complex dissociates at pH 4.0, and EsxA may then be freed to lyse (host) membranes (PubMed:17557817). Another study using recombinant protein did not find dissociation at acidic pH (PubMed:23150662). Recombinant heterodimer (with a His tag on EsxB) can be dissociated by the detergents amidosulfobetaine-14 and lauryldimethylamine N-oxide (PubMed:26260636).

Interacts with EspF (PubMed:19682254). An artificial EsxB-EsxA heterodimer interacts with EspA, EccB1, EccCa1, EccCb1, EspI, EspJ, EccA2 and EccE2; the latter 2 are from the adjacent ESX-2 locus (PubMed:19854905). Contributes to the heterodimer's interaction with EccCb1 (PubMed:19854905).

Interacts with host (mouse and human) TLR2 (PubMed:17486091, PubMed:20800577).

Interacts with host (human) beta-2-microglobulin (B2M) alone and in complex with EsxB; only binds free B2M and not B2M in complex with HLA-I (PubMed:25356553). The EsxA-EsxB-B2M complex can be detected in the host endoplasmic reticulum (PubMed:25356553). The B2M-EsxA complex can be detected in patients with pleural tuberculosis and is stable from pH 4.0 to 8.0 and in the presence of 2M NaCl (PubMed:25356553).

17 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
P9WNK521EBI-1253925,EBI-1253936

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-61227N

Protein interaction database and analysis system

More...
IntActi
P9WNK7, 2 interactors

Molecular INTeraction database

More...
MINTi
P9WNK7

STRING: functional protein association networks

More...
STRINGi
83332.Rv3875

<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

195
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
P9WNK7

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

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 – 95Not required for ESAT-6/CFP-10 complex to bind to host macrophage and monocytes1 PublicationAdd BLAST11

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili8 – 391 PublicationAdd BLAST32
Coiled coili56 – 87Sequence analysis1 PublicationAdd BLAST32

<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

May be secreted as a 4 coiled-coil complex with EsxB (PubMed:16048998).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 WXG100 family. ESAT-6 subfamily.1 Publication

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG4842 LUCA

KEGG Orthology (KO)

More...
KOi
K14956

Identification of Orthologs from Complete Genome Data

More...
OMAi
QAVQMRW

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036689 ESAT-6-like_sf
IPR010310 T7SS_ESAT-6-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06013 WXG100, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF140453 SSF140453, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03930 WXG100_ESAT6, 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.

P9WNK7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTEQQWNFAG IEAAASAIQG NVTSIHSLLD EGKQSLTKLA AAWGGSGSEA
60 70 80 90
YQGVQQKWDA TATELNNALQ NLARTISEAG QAMASTEGNV TGMFA
Length:95
Mass (Da):9,904
Last modified:April 16, 2014 - 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:i79BD529E3D88F519
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
X79562 Genomic DNA Translation: CAA56099.1
AF420491 Genomic DNA Translation: AAL16896.1
AY207398 Genomic DNA Translation: AAO62007.1
DQ451152 Genomic DNA Translation: ABD98021.1
DQ451153 Genomic DNA Translation: ABD98022.1
DQ451154 Genomic DNA Translation: ABD98023.1
DQ451155 Genomic DNA Translation: ABD98024.1
DQ451156 Genomic DNA Translation: ABD98025.1
DQ451157 Genomic DNA Translation: ABD98026.1
DQ451158 Genomic DNA Translation: ABD98027.1
DQ451159 Genomic DNA Translation: ABD98028.1
AL123456 Genomic DNA Translation: CCP46704.1
AF004671 Genomic DNA Translation: AAC83446.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A70803

NCBI Reference Sequences

More...
RefSeqi
WP_003399963.1, NZ_NVQJ01000074.1
YP_178023.1, NC_000962.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CCP46704; CCP46704; Rv3875

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
886209

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv3875

<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
X79562 Genomic DNA Translation: CAA56099.1
AF420491 Genomic DNA Translation: AAL16896.1
AY207398 Genomic DNA Translation: AAO62007.1
DQ451152 Genomic DNA Translation: ABD98021.1
DQ451153 Genomic DNA Translation: ABD98022.1
DQ451154 Genomic DNA Translation: ABD98023.1
DQ451155 Genomic DNA Translation: ABD98024.1
DQ451156 Genomic DNA Translation: ABD98025.1
DQ451157 Genomic DNA Translation: ABD98026.1
DQ451158 Genomic DNA Translation: ABD98027.1
DQ451159 Genomic DNA Translation: ABD98028.1
AL123456 Genomic DNA Translation: CCP46704.1
AF004671 Genomic DNA Translation: AAC83446.1
PIRiA70803
RefSeqiWP_003399963.1, NZ_NVQJ01000074.1
YP_178023.1, 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
1WA8NMR-B1-95[»]
3FAVX-ray2.15B/D2-95[»]
SMRiP9WNK7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-61227N
IntActiP9WNK7, 2 interactors
MINTiP9WNK7
STRINGi83332.Rv3875

PTM databases

iPTMnetiP9WNK7

Proteomic databases

PaxDbiP9WNK7

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P9WNK7

Genome annotation databases

EnsemblBacteriaiCCP46704; CCP46704; Rv3875
GeneIDi886209
KEGGimtu:Rv3875

Organism-specific databases

TubercuListiRv3875

Phylogenomic databases

eggNOGiCOG4842 LUCA
KOiK14956
OMAiQAVQMRW

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-8173-MONOMER

Family and domain databases

InterProiView protein in InterPro
IPR036689 ESAT-6-like_sf
IPR010310 T7SS_ESAT-6-like
PfamiView protein in Pfam
PF06013 WXG100, 1 hit
SUPFAMiSSF140453 SSF140453, 1 hit
TIGRFAMsiTIGR03930 WXG100_ESAT6, 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 nameiESXA_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: P9WNK7
Secondary accession number(s): F2GDN6
, O84901, P0A564, Q540D8, Q57165
<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: April 16, 2014
Last modified: October 16, 2019
This is version 34 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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