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6 kDa early secretory antigenic target (ESAT-6)

 ESXA_MYCTU              Reviewed;          95 AA.
P9WNK7; F2GDN6; O84901; P0A564; Q540D8; Q57165;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 26.
RecName: Full=6 kDa early secretory antigenic target {ECO:0000303|PubMed:7897219};
AltName: Full=ESAT-6;
Name=esxA {ECO:0000303|PubMed:19876390}; Synonyms=esaT6;
OrderedLocusNames=Rv3875; ORFNames=MTV027.10;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
BIOTECHNOLOGY.
STRAIN=H37Rv;
PubMed=7897219;
Andersen P., Andersen A.B., Sorensen A.L., Nagai S.;
"Recall of long-lived immunity to Mycobacterium tuberculosis infection
in mice.";
J. Immunol. 154:3359-3372(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
AND SUBCELLULAR LOCATION.
STRAIN=H37Rv;
PubMed=7729876;
Soerensen A.L., Nagai S., Houen G., Anderson P., Anderson A.B.;
"Purification and characterization of a low-molecular-mass T-cell
antigen secreted by Mycobacterium tuberculosis.";
Infect. Immun. 63:1710-1717(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Singh B., Siddiqui Z., Singh S., Sharma P.;
"ESAT-6 gene of a clinical isolate of Mycobacterium tuberculosis from
India.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lee C.F.;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1, 2, 3, 4, 5, and 6;
Dang D.A., Hoa T.M.T., Tran T.T.H., Nguyen T.N., Ho T.M.L.,
Nguyen V.H., Nguyen T.H.H.;
"Sequencing and analysis of the gene Esat6 of a Mycobacterium
tuberculosis isolate derived from a Vietnamese patient suffering lung
tuberculosis.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=7, and 8;
Dang D.A., Hoa T.M.T., Tran T.T.H., Nguyen T.N., Ho T.M.L.,
Nguyen V.H., Nguyen T.H.H.;
"Sequencing and analysis of the gene Esat6 of a Mycobacterium
tuberculosis isolate derived from a Vietnamese patient suffering
tuberculous meningitis.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71, AND INDUCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=9846755; DOI=10.1099/00221287-144-11-3195;
Berthet F.-X., Rasmussen P.B., Rosenkrands I., Andersen P.,
Gicquel B.;
"A Mycobacterium tuberculosis operon encoding ESAT-6 and a novel low-
molecular-mass culture filtrate protein (CFP-10).";
Microbiology 144:3195-3203(1998).
[9]
PROTEIN SEQUENCE OF 2-95, SUBUNIT, SUBCELLULAR LOCATION, MASS
SPECTROMETRY, ACETYLATION AT THR-2, AND PROTEOLYTIC CLEAVAGE.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=15378760; DOI=10.1002/pmic.200400906;
Okkels L.M., Mueller E.C., Schmid M., Rosenkrands I., Kaufmann S.H.,
Andersen P., Jungblut P.R.;
"CFP10 discriminates between nonacetylated and acetylated ESAT-6 of
Mycobacterium tuberculosis by differential interaction.";
Proteomics 4:2954-2960(2004).
[10]
FUNCTION, SUBUNIT, AND INTERACTION WITH ESXB.
STRAIN=ATCC 25618 / H37Rv;
PubMed=11940590; DOI=10.1074/jbc.M201625200;
Renshaw P.S., Panagiotidou P., Whelan A., Gordon S.V., Hewinson R.G.,
Williamson R.A., Carr M.D.;
"Conclusive evidence that the major T-cell antigens of the
Mycobacterium tuberculosis complex ESAT-6 and CFP-10 form a tight, 1:1
complex and characterization of the structural properties of ESAT-6,
CFP-10, and the ESAT-6*CFP-10 complex. Implications for pathogenesis
and virulence.";
J. Biol. Chem. 277:21598-21603(2002).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv, and ATCC 35801 / TMC 107 / Erdman;
PubMed=14557547; DOI=10.1073/pnas.1635213100;
Hsu T., Hingley-Wilson S.M., Chen B., Chen M., Dai A.Z., Morin P.M.,
Marks C.B., Padiyar J., Goulding C., Gingery M., Eisenberg D.,
Russell R.G., Derrick S.C., Collins F.M., Morris S.L., King C.H.,
Jacobs W.R. Jr.;
"The primary mechanism of attenuation of bacillus Calmette-Guerin is a
loss of secreted lytic function required for invasion of lung
interstitial tissue.";
Proc. Natl. Acad. Sci. U.S.A. 100:12420-12425(2003).
[12]
FUNCTION, INTERACTION WITH ESXB, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=14557536; DOI=10.1073/pnas.2235593100;
Stanley S.A., Raghavan S., Hwang W.W., Cox J.S.;
"Acute infection and macrophage subversion by Mycobacterium
tuberculosis require a specialized secretion system.";
Proc. Natl. Acad. Sci. U.S.A. 100:13001-13006(2003).
[13]
DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=14756778; DOI=10.1046/j.1365-2958.2003.03844.x;
Guinn K.M., Hickey M.J., Mathur S.K., Zakel K.L., Grotzke J.E.,
Lewinsohn D.M., Smith S., Sherman D.R.;
"Individual RD1-region genes are required for export of ESAT-6/CFP-10
and for virulence of Mycobacterium tuberculosis.";
Mol. Microbiol. 51:359-370(2004).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16030141; DOI=10.1073/pnas.0504922102;
Fortune S.M., Jaeger A., Sarracino D.A., Chase M.R., Sassetti C.M.,
Sherman D.R., Bloom B.R., Rubin E.J.;
"Mutually dependent secretion of proteins required for mycobacterial
virulence.";
Proc. Natl. Acad. Sci. U.S.A. 102:10676-10681(2005).
[15]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF THR-2;
GLN-4; PHE-8; ALA-14; 28-LEU-LEU-29; TRP-43; GLY-45; 55-GLN-GLN-56;
66-ASN-ASN-67; MET-83; VAL-90; MET-93 AND PHE-94, AND COILED COIL.
PubMed=16048998; DOI=10.1074/jbc.M503515200;
Brodin P., de Jonge M.I., Majlessi L., Leclerc C., Nilges M.,
Cole S.T., Brosch R.;
"Functional analysis of early secreted antigenic target-6, the
dominant T-cell antigen of Mycobacterium tuberculosis, reveals key
residues involved in secretion, complex formation, virulence, and
immunogenicity.";
J. Biol. Chem. 280:33953-33959(2005).
[16]
DISRUPTION PHENOTYPE.
PubMed=16368961; DOI=10.1128/IAI.74.1.88-98.2006;
Brodin P., Majlessi L., Marsollier L., de Jonge M.I., Bottai D.,
Demangel C., Hinds J., Neyrolles O., Butcher P.D., Leclerc C.,
Cole S.T., Brosch R.;
"Dissection of ESAT-6 system 1 of Mycobacterium tuberculosis and
impact on immunogenicity and virulence.";
Infect. Immun. 74:88-98(2006).
[17]
INTERACTION WITH ESXB.
PubMed=16973880; DOI=10.1126/science.1131167;
Champion P.A., Stanley S.A., Champion M.M., Brown E.J., Cox J.S.;
"C-terminal signal sequence promotes virulence factor secretion in
Mycobacterium tuberculosis.";
Science 313:1632-1636(2006).
[18]
FUNCTION IN APOPTOSIS, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17298391; DOI=10.1111/j.1462-5822.2007.00892.x;
Derrick S.C., Morris S.L.;
"The ESAT6 protein of Mycobacterium tuberculosis induces apoptosis of
macrophages by activating caspase expression.";
Cell. Microbiol. 9:1547-1555(2007).
[19]
FUNCTION IN HOST TLR INHIBITION, INTERACTION WITH HOST TLR2,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-43; 90-VAL--ALA-95;
90-VAL-PHE-94; VAL-90; MET-93 AND PHE-94.
PubMed=17486091; DOI=10.1038/ni1468;
Pathak S.K., Basu S., Basu K.K., Banerjee A., Pathak S.,
Bhattacharyya A., Kaisho T., Kundu M., Basu J.;
"Direct extracellular interaction between the early secreted antigen
ESAT-6 of Mycobacterium tuberculosis and TLR2 inhibits TLR signaling
in macrophages.";
Nat. Immunol. 8:610-618(2007).
[20]
ERRATUM.
PubMed=25689444; DOI=10.1038/ni0315-326b;
Pathak S.K., Basu S., Basu K.K., Banerjee A., Pathak S.,
Bhattacharyya A., Kaisho T., Kundu M., Basu J.;
"Corrigendum: Direct extracellular interaction between the early
secreted antigen ESAT-6 of Mycobacterium tuberculosis and TLR2
inhibits TLR signaling in macrophages.";
Nat. Immunol. 16:326-326(2015).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=17604718; DOI=10.1016/j.cell.2007.05.059;
van der Wel N., Hava D., Houben D., Fluitsma D., van Zon M.,
Pierson J., Brenner M., Peters P.J.;
"M. tuberculosis and M. leprae translocate from the phagolysosome to
the cytosol in myeloid cells.";
Cell 129:1287-1298(2007).
[22]
FUNCTION, SUBUNIT, AND MEMBRANE-BINDING.
PubMed=17557817; DOI=10.1128/JB.00469-07;
de Jonge M.I., Pehau-Arnaudet G., Fretz M.M., Romain F., Bottai D.,
Brodin P., Honore N., Marchal G., Jiskoot W., England P., Cole S.T.,
Brosch R.;
"ESAT-6 from Mycobacterium tuberculosis dissociates from its putative
chaperone CFP-10 under acidic conditions and exhibits membrane-lysing
activity.";
J. Bacteriol. 189:6028-6034(2007).
[23]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19265145; DOI=10.4049/jimmunol.0803579;
Wang X., Barnes P.F., Dobos-Elder K.M., Townsend J.C., Chung Y.T.,
Shams H., Weis S.E., Samten B.;
"ESAT-6 inhibits production of IFN-gamma by Mycobacterium
tuberculosis-responsive human T cells.";
J. Immunol. 182:3668-3677(2009).
[24]
INTERACTION WITH ESPF.
PubMed=19682254; DOI=10.1111/j.1365-2958.2009.06821.x;
DiGiuseppe Champion P.A., Champion M.M., Manzanillo P., Cox J.S.;
"ESX-1 secreted virulence factors are recognized by multiple cytosolic
AAA ATPases in pathogenic mycobacteria.";
Mol. Microbiol. 73:950-962(2009).
[25]
NOMENCLATURE.
PubMed=19876390; DOI=10.1371/journal.ppat.1000507;
Bitter W., Houben E.N., Bottai D., Brodin P., Brown E.J., Cox J.S.,
Derbyshire K., Fortune S.M., Gao L.Y., Liu J., Gey van Pittius N.C.,
Pym A.S., Rubin E.J., Sherman D.R., Cole S.T., Brosch R.;
"Systematic genetic nomenclature for type VII secretion systems.";
PLoS Pathog. 5:E1000507-E1000507(2009).
[26]
INTERACTION WITH HOST TLR2.
PubMed=20800577; DOI=10.1016/j.bbrc.2010.08.085;
Chambers M.A., Whelan A.O., Spallek R., Singh M., Coddeville B.,
Guerardel Y., Elass E.;
"Non-acylated Mycobacterium bovis glycoprotein MPB83 binds to TLR1/2
and stimulates production of matrix metalloproteinase 9.";
Biochem. Biophys. Res. Commun. 400:403-408(2010).
[27]
SUBUNIT, AND MUTAGENESIS OF GLU-87.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19854905; DOI=10.1128/JB.01032-09;
Callahan B., Nguyen K., Collins A., Valdes K., Caplow M.,
Crossman D.K., Steyn A.J., Eisele L., Derbyshire K.M.;
"Conservation of structure and protein-protein interactions mediated
by the secreted mycobacterial proteins EsxA, EsxB, and EspA.";
J. Bacteriol. 192:326-335(2010).
[28]
FUNCTION IN PNEUMOCYTE CYTOTOXICITY, SUBCELLULAR LOCATION, SUBUNIT,
AND INDUCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19906174; DOI=10.1111/j.1365-2958.2009.06959.x;
Kinhikar A.G., Verma I., Chandra D., Singh K.K., Weldingh K.,
Andersen P., Hsu T., Jacobs W.R. Jr., Laal S.;
"Potential role for ESAT6 in dissemination of M. tuberculosis via
human lung epithelial cells.";
Mol. Microbiol. 75:92-106(2010).
[29]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=20148899; DOI=10.1111/j.1462-5822.2010.01450.x;
Mishra B.B., Moura-Alves P., Sonawane A., Hacohen N., Griffiths G.,
Moita L.F., Anes E.;
"Mycobacterium tuberculosis protein ESAT-6 is a potent activator of
the NLRP3/ASC inflammasome.";
Cell. Microbiol. 12:1046-1063(2010).
[30]
FUNCTION.
PubMed=21586573; DOI=10.1074/jbc.M111.234062;
Peng H., Wang X., Barnes P.F., Tang H., Townsend J.C., Samten B.;
"The Mycobacterium tuberculosis early secreted antigenic target of 6
kDa inhibits T cell interferon-gamma production through the p38
mitogen-activated protein kinase pathway.";
J. Biol. Chem. 286:24508-24518(2011).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[32]
FUNCTION IN HOST PHAGOSOME LYSIS, DISRUPTION PHENOTYPE, AND
MUTAGENESIS OF 84-ALA--ALA-95.
STRAIN=ATCC 25618 / H37Rv;
PubMed=22319448; DOI=10.1371/journal.ppat.1002507;
Simeone R., Bobard A., Lippmann J., Bitter W., Majlessi L., Brosch R.,
Enninga J.;
"Phagosomal rupture by Mycobacterium tuberculosis results in toxicity
and host cell death.";
PLoS Pathog. 8:E1002507-E1002507(2012).
[33]
FUNCTION, AND MUTAGENESIS OF 84-ALA--ALA-95.
PubMed=22524898; DOI=10.1111/j.1462-5822.2012.01799.x;
Houben D., Demangel C., van Ingen J., Perez J., Baldeon L.,
Abdallah A.M., Caleechurn L., Bottai D., van Zon M., de Punder K.,
van der Laan T., Kant A., Bossers-de Vries R., Willemsen P.,
Bitter W., van Soolingen D., Brosch R., van der Wel N., Peters P.J.;
"ESX-1-mediated translocation to the cytosol controls virulence of
mycobacteria.";
Cell. Microbiol. 14:1287-1298(2012).
[34]
FUNCTION, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=23150662; DOI=10.1074/jbc.M112.420869;
De Leon J., Jiang G., Ma Y., Rubin E., Fortune S., Sun J.;
"Mycobacterium tuberculosis ESAT-6 exhibits a unique membrane-
interacting activity that is not found in its ortholog from non-
pathogenic Mycobacterium smegmatis.";
J. Biol. Chem. 287:44184-44191(2012).
[35]
POSSIBLE FUNCTION IN APOPTOSIS AND HOST INFECTION, AND INDUCTION.
STRAIN=ATCC 25618 / H37Rv, and MT103;
PubMed=23848406; DOI=10.1111/cmi.12169;
Aguilo J.I., Alonso H., Uranga S., Marinova D., Arbues A.,
de Martino A., Anel A., Monzon M., Badiola J., Pardo J., Brosch R.,
Martin C.;
"ESX-1-induced apoptosis is involved in cell-to-cell spread of
Mycobacterium tuberculosis.";
Cell. Microbiol. 15:1994-2005(2013).
[36]
FUNCTION.
PubMed=23867456; DOI=10.1074/jbc.M112.448217;
Boggaram V., Gottipati K.R., Wang X., Samten B.;
"Early secreted antigenic target of 6 kDa (ESAT-6) protein of
Mycobacterium tuberculosis induces interleukin-8 (IL-8) expression in
lung epithelial cells via protein kinase signaling and reactive oxygen
species.";
J. Biol. Chem. 288:25500-25511(2013).
[37]
SECRETION INDUCTION BY ZINC, AND SECRETION INHIBITION.
PubMed=25299337; DOI=10.1016/j.chom.2014.09.008;
Rybniker J., Chen J.M., Sala C., Hartkoorn R.C., Vocat A., Benjak A.,
Boy-Roettger S., Zhang M., Szekely R., Greff Z., Orfi L.,
Szabadkai I., Pato J., Keri G., Cole S.T.;
"Anticytolytic screen identifies inhibitors of mycobacterial virulence
protein secretion.";
Cell Host Microbe 16:538-548(2014).
[38]
FUNCTION IN NEUTROPHIL NECROSIS.
PubMed=25321481; DOI=10.1038/cddis.2014.394;
Francis R.J., Butler R.E., Stewart G.R.;
"Mycobacterium tuberculosis ESAT-6 is a leukocidin causing Ca2+
influx, necrosis and neutrophil extracellular trap formation.";
Cell Death Dis. 5:E1474-E1474(2014).
[39]
FUNCTION, INTERACTION WITH HOST B2M, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 90-VAL--ALA-95.
PubMed=25356553; DOI=10.1371/journal.ppat.1004446;
Sreejit G., Ahmed A., Parveen N., Jha V., Valluri V.L., Ghosh S.,
Mukhopadhyay S.;
"The ESAT-6 protein of Mycobacterium tuberculosis interacts with beta-
2-microglobulin (beta2M) affecting antigen presentation function of
macrophage.";
PLoS Pathog. 10:E1004446-E1004446(2014).
[40]
FUNCTION IN PORE FORMATION, SUBCELLULAR LOCATION, TOPOLOGY, AND
MUTAGENESIS OF 1-MET--GLY-10; ASN-21; GLN-34; SER-35; THR-37; GLY-45;
GLN-55; TRP-58; ALA-60 AND 86-THR--ALA-95.
PubMed=25645924; DOI=10.1074/jbc.M114.622076;
Ma Y., Keil V., Sun J.;
"Characterization of Mycobacterium tuberculosis EsxA membrane
insertion: roles of N- and C-terminal flexible arms and central helix-
turn-helix motif.";
J. Biol. Chem. 290:7314-7322(2015).
[41]
FUNCTION.
STRAIN=H37Rv;
PubMed=26048138; DOI=10.1016/j.chom.2015.05.003;
Wassermann R., Gulen M.F., Sala C., Perin S.G., Lou Y., Rybniker J.,
Schmid-Burgk J.L., Schmidt T., Hornung V., Cole S.T., Ablasser A.;
"Mycobacterium tuberculosis differentially activates cGAS- and
inflammasome-dependent intracellular immune responses through ESX-1.";
Cell Host Microbe 17:799-810(2015).
[42]
FUNCTION.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=26048136; DOI=10.1016/j.chom.2015.05.004;
Watson R.O., Bell S.L., MacDuff D.A., Kimmey J.M., Diner E.J.,
Olivas J., Vance R.E., Stallings C.L., Virgin H.W., Cox J.S.;
"The cytosolic sensor cGAS detects Mycobacterium tuberculosis DNA to
induce type I interferons and activate autophagy.";
Cell Host Microbe 17:811-819(2015).
[43]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv, and ATCC 35801 / TMC 107 / Erdman;
PubMed=26092385; DOI=10.1016/j.micinf.2015.06.003;
Fine-Coulson K., Giguere S., Quinn F.D., Reaves B.J.;
"Infection of A549 human type II epithelial cells with Mycobacterium
tuberculosis induces changes in mitochondrial morphology, distribution
and mass that are dependent on the early secreted antigen, ESAT-6.";
Microbes Infect. 17:689-697(2015).
[44]
FUNCTION, AND SUBUNIT.
PubMed=26260636; DOI=10.1111/febs.13408;
Refai A., Haoues M., Othman H., Barbouche M.R., Moua P., Bondon A.,
Mouret L., Srairi-Abid N., Essafi M.;
"Two distinct conformational states of Mycobacterium tuberculosis
virulent factor early secreted antigenic target 6 kDa are behind the
discrepancy around its biological functions.";
FEBS J. 282:4114-4129(2015).
[45]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-17;
25-ILE-HIS-26; HIS-26; LYS-38; ASN-67 AND ARG-74.
PubMed=26801203; DOI=10.1002/1873-3468.12072;
Peng X., Jiang G., Liu W., Zhang Q., Qian W., Sun J.;
"Characterization of differential pore-forming activities of ESAT-6
proteins from Mycobacterium tuberculosis and Mycobacterium
smegmatis.";
FEBS Lett. 590:509-519(2016).
[46]
REVIEW.
PubMed=26456678; DOI=10.1016/j.toxicon.2015.10.003;
Peng X., Sun J.;
"Mechanism of ESAT-6 membrane interaction and its roles in
pathogenesis of Mycobacterium tuberculosis.";
Toxicon 116:29-34(2016).
[47]
PRELIMINARY X-RAY CRYSTALLOGRAPHY, AND SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20085764; DOI=10.1016/j.febslet.2009.12.057;
Poulsen C., Holton S., Geerlof A., Wilmanns M., Song Y.H.;
"Stoichiometric protein complex formation and over-expression using
the prokaryotic native operon structure.";
FEBS Lett. 584:669-674(2010).
[48]
STRUCTURE BY NMR IN COMPLEX WITH CFP-10 (ESXB), SUBUNIT, SUBCELLULAR
LOCATION, AND DOMAIN.
PubMed=15973432; DOI=10.1038/sj.emboj.7600732;
Renshaw P.S., Lightbody K.L., Veverka V., Muskett F.W., Kelly G.,
Frenkiel T.A., Gordon S.V., Hewinson R.G., Burke B., Norman J.,
Williamson R.A., Carr M.D.;
"Structure and function of the complex formed by the tuberculosis
virulence factors CFP-10 and ESAT-6.";
EMBO J. 24:2491-2498(2005).
[49]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-95 IN COMPLEX WITH CFP-10
(ESXB).
STRAIN=H37Rv;
PubMed=24586681; DOI=10.1371/journal.pone.0089313;
Poulsen C., Panjikar S., Holton S.J., Wilmanns M., Song Y.H.;
"WXG100 protein superfamily consists of three subfamilies and exhibits
an alpha-helical C-terminal conserved residue pattern.";
PLoS ONE 9:E89313-E89313(2014).
-!- FUNCTION: 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 uM) 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). {ECO:0000250|UniProtKB:D1A4H1,
ECO:0000269|PubMed:11940590, ECO:0000269|PubMed:14557536,
ECO:0000269|PubMed:14557547, ECO:0000269|PubMed:17298391,
ECO:0000269|PubMed:17486091, ECO:0000269|PubMed:17557817,
ECO:0000269|PubMed:17604718, ECO:0000269|PubMed:19265145,
ECO:0000269|PubMed:19906174, ECO:0000269|PubMed:20148899,
ECO:0000269|PubMed:21586573, ECO:0000269|PubMed:22319448,
ECO:0000269|PubMed:23867456, ECO:0000269|PubMed:25321481,
ECO:0000269|PubMed:25356553, ECO:0000269|PubMed:26092385,
ECO:0000269|PubMed:26260636, ECO:0000269|PubMed:7729876,
ECO:0000269|PubMed:7897219, ECO:0000305|PubMed:23848406}.
-!- FUNCTION: 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). {ECO:0000269|PubMed:26048136,
ECO:0000269|PubMed:26048138}.
-!- SUBUNIT: 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). {ECO:0000269|PubMed:11940590,
ECO:0000269|PubMed:14557536, ECO:0000269|PubMed:15378760,
ECO:0000269|PubMed:15973432, ECO:0000269|PubMed:16048998,
ECO:0000269|PubMed:16973880, ECO:0000269|PubMed:17486091,
ECO:0000269|PubMed:17557817, ECO:0000269|PubMed:19682254,
ECO:0000269|PubMed:19854905, ECO:0000269|PubMed:19906174,
ECO:0000269|PubMed:20085764, ECO:0000269|PubMed:20800577,
ECO:0000269|PubMed:23150662, ECO:0000269|PubMed:24586681,
ECO:0000269|PubMed:25356553, ECO:0000269|PubMed:26260636}.
-!- INTERACTION:
P9WNK5:esxB; NbExp=21; IntAct=EBI-1253925, EBI-1253936;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14557536,
ECO:0000269|PubMed:14557547, ECO:0000269|PubMed:15378760,
ECO:0000269|PubMed:16030141, ECO:0000269|PubMed:16048998,
ECO:0000269|PubMed:7729876, ECO:0000269|PubMed:7897219}. Secreted,
cell wall {ECO:0000269|PubMed:19906174}. Host cell surface
{ECO:0000269|PubMed:15973432, ECO:0000269|PubMed:17486091,
ECO:0000269|PubMed:19265145}. Host cytoplasm
{ECO:0000269|PubMed:20148899}. Host endoplasmic reticulum
{ECO:0000269|PubMed:25356553}. Host cell membrane
{ECO:0000305|PubMed:25645924, ECO:0000305|PubMed:26801203}.
Note=Probably secreted via the ESX-1 / type VII secretion system
(T7SS) (PubMed:19876390). Secreted protein binds to bacterial cell
wall (PubMed:19906174). Binds to host (mouse) TLR2 on the cell
surface (PubMed:17486091). Binds to CD4+, CD8+, CD14+ and CD19+
host (human) cells (PubMed:19265145). Localized on the cell
surface of host (human) cell monocytes and macrophages (often in
patches), but not fibroblasts (PubMed:15973432). Exogenous EsxA
and EsxA-EsxB complex can enter host (human and mouse) endoplasmic
reticulum, where they bind beta-2-microglobulin (PubMed:25356553).
At acidic pH able to form pores in artificial membranes, might
form pores in host phagosome membranes in absence of EsxB,
allowing escape of bacteria into the host cytoplasm
(PubMed:25645924, PubMed:26801203). The central pair of alpha
helices probably insert into the membrane while the N- and C-
terminal arms do not, but may rest on the membrane surface as they
are required for membrane insertion (PubMed:25645924).
{ECO:0000269|PubMed:15973432, ECO:0000269|PubMed:17486091,
ECO:0000269|PubMed:19265145, ECO:0000269|PubMed:19876390,
ECO:0000269|PubMed:19906174, ECO:0000269|PubMed:25356553,
ECO:0000269|PubMed:25645924, ECO:0000305|PubMed:25645924,
ECO:0000305|PubMed:26801203}.
-!- INDUCTION: 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 Zn(2+), the physiological concentration in
macrophages, induces 6-fold more secreted protein
(PubMed:25299337). Part of the esxB-esxA operon (PubMed:9846755).
{ECO:0000269|PubMed:19906174, ECO:0000269|PubMed:23848406,
ECO:0000269|PubMed:25299337, ECO:0000269|PubMed:9846755}.
-!- DOMAIN: May be secreted as a 4 coiled-coil complex with EsxB
(PubMed:16048998). {ECO:0000269|PubMed:16048998}.
-!- PTM: 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). {ECO:0000269|PubMed:15378760}.
-!- DISRUPTION PHENOTYPE: 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). {ECO:0000269|PubMed:14557536,
ECO:0000269|PubMed:14557547, ECO:0000269|PubMed:14756778,
ECO:0000269|PubMed:16030141, ECO:0000269|PubMed:16368961,
ECO:0000269|PubMed:17604718, ECO:0000269|PubMed:20148899,
ECO:0000269|PubMed:22319448, ECO:0000269|PubMed:26092385}.
-!- BIOTECHNOLOGY: A good candiate for vaccine development
(PubMed:7897219). It has been tested in a number of experimental
situations. {ECO:0000305|PubMed:7897219}.
-!- 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 resposible 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).
{ECO:0000269|PubMed:14557547, ECO:0000269|PubMed:14756778,
ECO:0000269|PubMed:16368961, ECO:0000269|PubMed:17298391,
ECO:0000269|PubMed:22319448, ECO:0000269|PubMed:22524898}.
-!- MISCELLANEOUS: Secretion of EspA, EsxA and EsxB is mutually
dependent (PubMed:16030141). {ECO:0000269|PubMed:16030141}.
-!- MISCELLANEOUS: 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). {ECO:0000269|PubMed:19854905}.
-!- MISCELLANEOUS: 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). {ECO:0000269|PubMed:25299337}.
-!- SIMILARITY: Belongs to the WXG100 family. ESAT-6 subfamily.
{ECO:0000305|PubMed:19876390}.
-----------------------------------------------------------------------
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EMBL; X79562; CAA56099.1; -; Genomic_DNA.
EMBL; AF420491; AAL16896.1; -; Genomic_DNA.
EMBL; AY207398; AAO62007.1; -; Genomic_DNA.
EMBL; DQ451152; ABD98021.1; -; Genomic_DNA.
EMBL; DQ451153; ABD98022.1; -; Genomic_DNA.
EMBL; DQ451154; ABD98023.1; -; Genomic_DNA.
EMBL; DQ451155; ABD98024.1; -; Genomic_DNA.
EMBL; DQ451156; ABD98025.1; -; Genomic_DNA.
EMBL; DQ451157; ABD98026.1; -; Genomic_DNA.
EMBL; DQ451158; ABD98027.1; -; Genomic_DNA.
EMBL; DQ451159; ABD98028.1; -; Genomic_DNA.
EMBL; AL123456; CCP46704.1; -; Genomic_DNA.
EMBL; AF004671; AAC83446.1; -; Genomic_DNA.
PIR; A70803; A70803.
RefSeq; WP_003399963.1; NZ_KK339374.1.
RefSeq; YP_178023.1; NC_000962.3.
PDB; 1WA8; NMR; -; B=1-95.
PDB; 3FAV; X-ray; 2.15 A; B/D=2-95.
PDBsum; 1WA8; -.
PDBsum; 3FAV; -.
ProteinModelPortal; P9WNK7; -.
SMR; P9WNK7; -.
DIP; DIP-61227N; -.
IntAct; P9WNK7; 2.
STRING; 83332.Rv3875; -.
iPTMnet; P9WNK7; -.
PaxDb; P9WNK7; -.
EnsemblBacteria; CCP46704; CCP46704; Rv3875.
GeneID; 886209; -.
KEGG; mtu:Rv3875; -.
TubercuList; Rv3875; -.
eggNOG; COG4842; LUCA.
KO; K14956; -.
OMA; FNQNTEG; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005737; C:cytoplasm; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0046812; F:host cell surface binding; IDA:MTBBASE.
GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
GO; GO:0052027; P:modulation by symbiont of host signal transduction pathway; IDA:MTBBASE.
GO; GO:0052083; P:negative regulation by symbiont of host cell-mediated immune response; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IMP:MTBBASE.
GO; GO:0044315; P:protein secretion by the type VII secretion system; IMP:MTBBASE.
InterPro; IPR036689; ESAT-6-like_sf.
InterPro; IPR010310; T7SS_ESAT-6-like.
Pfam; PF06013; WXG100; 1.
SUPFAM; SSF140453; SSF140453; 1.
TIGRFAMs; TIGR03930; WXG100_ESAT6; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Cell wall; Coiled coil;
Complete proteome; Direct protein sequencing; Host cell membrane;
Host cytoplasm; Host endoplasmic reticulum; Host membrane; Membrane;
Reference proteome; Secreted; Transmembrane; Transmembrane helix;
Virulence.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609,
ECO:0000269|PubMed:15378760,
ECO:0000269|PubMed:7729876}.
CHAIN 2 95 6 kDa early secretory antigenic target.
/FTId=PRO_0000167793.
TRANSMEM 11 43 Helical. {ECO:0000305|PubMed:25645924}.
TRANSMEM 49 85 Helical. {ECO:0000305|PubMed:25645924}.
REGION 85 95 Not required for ESAT-6/CFP-10 complex to
bind to host macrophage and monocytes.
{ECO:0000269|PubMed:15973432}.
COILED 8 39 {ECO:0000305|PubMed:16048998}.
COILED 56 87 {ECO:0000255,
ECO:0000305|PubMed:16048998}.
MOD_RES 2 2 N-acetylthreonine; partial.
{ECO:0000244|PubMed:21969609,
ECO:0000269|PubMed:15378760}.
MUTAGEN 2 10 Missing: 40% reduction in liposome
disruption. 80% reduction; when
associated with 86-T--A-95.
{ECO:0000269|PubMed:25645924}.
MUTAGEN 2 2 T->H: Wild-type virulence in an esxA
deletion strain; protein should not be
acetylated.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 4 4 Q->L: Wild-type virulence in an esxA
deletion strain.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 8 8 F->I: Wild-type virulence in an esxA
deletion strain.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 14 14 A->R: Wild-type virulence in an esxA
deletion strain.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 17 17 A->E: 88% reduction in liposome
disruption; when associated with 25-T-A-
26. {ECO:0000269|PubMed:26801203}.
MUTAGEN 21 21 N->C: Cannot be overproduced and
purified. {ECO:0000269|PubMed:25645924}.
MUTAGEN 25 26 IH->TA: 40% reduction in liposome
disruption. 88% reduction in liposome
disruption; when associated with E-17.
Reduced liposome disruption; when
associated with T-38.
{ECO:0000269|PubMed:26801203}.
MUTAGEN 26 26 H->A: 16% reduction in liposome
disruption.
{ECO:0000269|PubMed:26801203}.
MUTAGEN 28 29 LL->AS: Does not restore virulence in an
esxA deletion strain, decreased secretion
of EsxA and EsxB.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 34 34 Q->C: NBD-linked protein does not
fluoresce at acidic pH in presence of
liposomes, this residue may face inwards
in membranes away from lipids.
{ECO:0000269|PubMed:25645924}.
MUTAGEN 35 35 S->C: NBD-linked protein fluoresces at
acidic pH in presence of liposomes,
suggests this residue faces lipids.
{ECO:0000269|PubMed:25645924}.
MUTAGEN 37 37 T->C: NBD-linked protein does not
fluoresce at acidic pH in presence of
liposomes, this residue may face inwards
in membranes away from lipids.
{ECO:0000269|PubMed:25645924}.
MUTAGEN 38 38 K->T: Reduced liposome disruption; when
associated with 25-T-A-26.
{ECO:0000269|PubMed:26801203}.
MUTAGEN 43 43 W->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.
{ECO:0000269|PubMed:16048998,
ECO:0000269|PubMed:17486091}.
MUTAGEN 45 45 G->C: NBD-linked protein moderately
fluoresces at acidic pH in presence of
liposomes, suggests this residue is
partially within membrane.
{ECO:0000269|PubMed:25645924}.
MUTAGEN 45 45 G->T: Does not restore virulence in an
esxA deletion strain, wild-type secretion
of EsxA and EsxB.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 55 56 QQ->IA: Wild-type virulence in an esxA
deletion strain.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 55 55 Q->C: NBD-linked protein does not
fluoresce at acidic pH in presence of
liposomes, this residue may face inwards
in membranes away from lipids.
{ECO:0000269|PubMed:25645924}.
MUTAGEN 58 58 W->C: Cannot be overproduced and
purified. {ECO:0000269|PubMed:25645924}.
MUTAGEN 60 60 A->C: NBD-linked protein fluoresces at
acidic pH in presence of liposomes,
suggests this residue faces lipids.
{ECO:0000269|PubMed:25645924}.
MUTAGEN 66 67 NN->IA: Wild-type virulence in an esxA
deletion strain.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 67 67 N->L: Reduced liposome disruption; when
associated with 25-T-A-26.
{ECO:0000269|PubMed:26801203}.
MUTAGEN 74 74 R->Q: Reduced liposome disruption; when
associated with 25-T-A-26.
{ECO:0000269|PubMed:26801203}.
MUTAGEN 83 83 M->I: Wild-type virulence in an esxA
deletion strain.
{ECO:0000269|PubMed:16048998}.
MUTAGEN 84 95 Missing: Bacteria no longer gain access
to host cytoplasm via phagosomal rupture.
{ECO:0000269|PubMed:22319448,
ECO:0000269|PubMed:22524898}.
MUTAGEN 86 95 Missing: 40% reduction in liposome
disruption. 80% reduction; when
associated with 2-T--G-10.
{ECO:0000269|PubMed:25645924}.
MUTAGEN 87 87 E->K: Abolishes EsxB-EsxA heterodimer
interaction with EccCb1, maintains
interaction with EspA, EccA2 and EccE2.
{ECO:0000269|PubMed:19854905}.
MUTAGEN 90 95 Missing: 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).
{ECO:0000269|PubMed:17486091,
ECO:0000269|PubMed:25356553}.
MUTAGEN 90 94 VTGMF->RTGTQ: No longer inhibits host
TLR2-signaling.
{ECO:0000269|PubMed:17486091}.
MUTAGEN 90 90 V->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).
{ECO:0000269|PubMed:16048998,
ECO:0000269|PubMed:17486091}.
MUTAGEN 93 93 M->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).
{ECO:0000269|PubMed:16048998,
ECO:0000269|PubMed:17486091}.
MUTAGEN 94 94 F->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).
{ECO:0000269|PubMed:16048998,
ECO:0000269|PubMed:17486091}.
HELIX 11 38 {ECO:0000244|PDB:3FAV}.
HELIX 39 43 {ECO:0000244|PDB:3FAV}.
STRAND 46 48 {ECO:0000244|PDB:1WA8}.
HELIX 49 80 {ECO:0000244|PDB:3FAV}.
TURN 82 85 {ECO:0000244|PDB:1WA8}.
TURN 91 93 {ECO:0000244|PDB:1WA8}.
SEQUENCE 95 AA; 9904 MW; 79BD529E3D88F519 CRC64;
MTEQQWNFAG IEAAASAIQG NVTSIHSLLD EGKQSLTKLA AAWGGSGSEA YQGVQQKWDA
TATELNNALQ NLARTISEAG QAMASTEGNV TGMFA


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