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ESAT-6-like protein EsxB (10 kDa culture filtrate antigen CFP-10) (CFP-10) (Secreted antigenic protein MTSA-10)

 ESXB_MYCTU              Reviewed;         100 AA.
P9WNK5; L0TDT9; O69739; P0A566;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 28.
RecName: Full=ESAT-6-like protein EsxB;
AltName: Full=10 kDa culture filtrate antigen CFP-10 {ECO:0000303|PubMed:9846755};
Short=CFP-10;
AltName: Full=Secreted antigenic protein MTSA-10;
Name=esxB {ECO:0000303|PubMed:19876390};
Synonyms=cfp10, lhp {ECO:0000303|PubMed:9846755},
mtsA10 {ECO:0000303|Ref.2}; OrderedLocusNames=Rv3874;
ORFNames=MTV027.09;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16,
SUBCELLULAR LOCATION, 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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Singh B., Siddiqui Z., Singh S., Sharma P.;
"Rv3874 (mtsa-10) gene of a clinical isolate of Mycobacterium
tuberculosis from India.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
FUNCTION, SUBUNIT, AND INTERACTION WITH ESXA.
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).
[5]
FUNCTION, 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).
[6]
INTERACTION WITH ESXA AND ECCCB1, AND SUBCELLULAR LOCATION.
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).
[7]
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).
[8]
SUBUNIT, AND SUBCELLULAR LOCATION.
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).
[9]
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).
[10]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, 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).
[11]
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).
[12]
INTERACTION WITH ESXA AND ECCCB1, DOMAIN, AND MUTAGENESIS OF LEU-94;
SER-96; MET-98; GLY-99 AND PHE-100.
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).
[13]
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).
[14]
FUNCTION, AND SUBUNIT.
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).
[15]
INTERACTION WITH PPE68.
PubMed=17433643; DOI=10.1016/j.micres.2006.11.016;
Teutschbein J., Schumann G., Mollmann U., Grabley S., Cole S.T.,
Munder T.;
"A protein linkage map of the ESAT-6 secretion system 1 (ESX-1) of
Mycobacterium tuberculosis.";
Microbiol. Res. 164:253-259(2009).
[16]
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).
[17]
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).
[18]
SUBUNIT, AND MUTAGENESIS OF GLN-42; ALA-62 AND SER-95.
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).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
[21]
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).
[22]
INTERACTION WITH HOST B2M, AND SUBCELLULAR LOCATION.
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).
[23]
FUNCTION IN NEUTROPHIL ACTIVATION.
PubMed=25332123; DOI=10.1128/IAI.02493-14;
Welin A., Bjoernsdottir H., Winther M., Christenson K., Oprea T.,
Karlsson A., Forsman H., Dahlgren C., Bylund J.;
"CFP-10 from Mycobacterium tuberculosis selectively activates human
neutrophils through a pertussis toxin-sensitive chemotactic
receptor.";
Infect. Immun. 83:205-213(2015).
[24]
POSSIBLE FUNCTION, AND INTERACTION WITH ECCCB1.
PubMed=25865481; DOI=10.1016/j.cell.2015.03.040;
Rosenberg O.S., Dovala D., Li X., Connolly L., Bendebury A.,
Finer-Moore J., Holton J., Cheng Y., Stroud R.M., Cox J.S.;
"Substrates control multimerization and activation of the multi-domain
ATPase motor of type VII secretion.";
Cell 161:501-512(2015).
[25]
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).
[26]
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).
[27]
STRUCTURE BY NMR OF 2-100 IN COMPLEX WITH ESAT-6 (ESXA), SUBUNIT, AND
SUBCELLULAR LOCATION.
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).
[28]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH ESAT-6 (ESXA).
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. Acts as a strong host (human) T-cell
antigen (PubMed:11940590). Involved in translocation of bacteria
from the host (human) phagolysosome to the host cytoplasm
(PubMed:17604718). Might serve as a chaperone to prevent
uncontrolled membrane lysis by its partner EsxA; native protein
binds poorly to artificial liposomes in the absence or presence of
EsxA (PubMed:17557817, PubMed:26260636). EsxA and EsxA-EsxB are
cytotoxic to pneumocytes (PubMed:19906174). EsxB (and EsxA-EsxB
but not EsxA alone) activates human neutrophils; EsxB transiently
induces host (human) intracellular Ca(2+) mobility in a dose-
dependent manner, monocytes and lymphocytes do not respond
(PubMed:25332123). Neutrophils respond to EsxB by chemotaxis and
primed neutrophils treated with EsxB produce reactive oxygen
species (ROS); Ca(2+) release and the ROS burst via are induced by
an unidentified G-protein coupled receptor (PubMed:25332123). May
help regulate assembly and function of the type VII secretion
system (T7SS) (PubMed:25865481). {ECO:0000269|PubMed:11940590,
ECO:0000269|PubMed:17557817, ECO:0000269|PubMed:17604718,
ECO:0000269|PubMed:19906174, ECO:0000269|PubMed:25332123,
ECO:0000269|PubMed:25865481, ECO:0000305|PubMed:26260636}.
-!- SUBUNIT: Able to form a homodimer (By similarity). Forms a tight
1:1 complex with EsxA (ESAT-6) (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). In vitro EsxB
only interacts with non-acetylated EsxA; it 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 then lyse 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 EccCb1 (PubMed:14557536,
PubMed:16973880, PubMed:25865481). Interacts with PPE68
(PubMed:17433643). Interacts with EccCa1, EccCb1, EsxA, EspI and
EspJ (PubMed:19854905). 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). Interacts with host (human) beta-2-
microglobulin (B2M) in complex with EsxA; only binds free B2M and
not B2M in complex with HLA-I (PubMed:25356553).
{ECO:0000250|UniProtKB:D1A4H0, ECO:0000269|PubMed:11940590,
ECO:0000269|PubMed:14557536, ECO:0000269|PubMed:15973432,
ECO:0000269|PubMed:16048998, ECO:0000269|PubMed:16973880,
ECO:0000269|PubMed:17433643, ECO:0000269|PubMed:17557817,
ECO:0000269|PubMed:19854905, ECO:0000269|PubMed:19906174,
ECO:0000269|PubMed:20085764, ECO:0000269|PubMed:23150662,
ECO:0000269|PubMed:24586681, ECO:0000269|PubMed:25356553,
ECO:0000269|PubMed:25865481, ECO:0000269|PubMed:26260636}.
-!- INTERACTION:
P9WPC9:clpC1; NbExp=3; IntAct=EBI-1253936, EBI-1254029;
P9WNB1:eccCb1; NbExp=3; IntAct=EBI-1253936, EBI-6514882;
P9WNK7:esxA; NbExp=21; IntAct=EBI-1253936, EBI-1253925;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14557536,
ECO:0000269|PubMed:15378760, ECO:0000269|PubMed:16048998,
ECO:0000269|PubMed:9846755}. Secreted, cell wall
{ECO:0000269|PubMed:19906174}. Host cell surface
{ECO:0000269|PubMed:15973432, ECO:0000269|PubMed:19265145}. Host
endoplasmic reticulum {ECO:0000269|PubMed:25356553}. Note=Probably
secreted via the ESX-1 / type VII secretion system (T7SS)
(PubMed:19876390). Binds to 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
(PubMed:25356553). {ECO:0000269|PubMed:15973432,
ECO:0000269|PubMed:19265145, ECO:0000269|PubMed:19876390,
ECO:0000269|PubMed:25356553}.
-!- INDUCTION: Constitutively expressed, part of the esxB-esxA operon
(PubMed:9846755). {ECO:0000269|PubMed:9846755}.
-!- DOMAIN: May be secreted as a 4 coiled-coil complex with EsxA
(PubMed:16048998). The C-terminal domain is required for
interaction with both EsxA and EccCb1; the last 7 amino acids are
necessary and sufficient for EccCb1 binding and secretion
(PubMed:16973880). {ECO:0000269|PubMed:16048998,
ECO:0000269|PubMed:16973880}.
-!- DISRUPTION PHENOTYPE: Bacteria no longer translocate from the
phagolysosome to the cytosol of host (human) cells probably due to
polar effects on the downstream esxA gene; bacteria replicate in
phagolysosome, decreased apoptosis of infected host (human)
dendritic cells (PubMed:17604718). Loss of ability to lyse host
(human) lung epithelial cells, possibly due to polar effects on
the downstream esxA 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). Inactivation leads to absence of
EsxA and EsxB from cell lysates (PubMed:14756778,
PubMed:16368961). No secretion of EspA (PubMed:16030141).
{ECO:0000269|PubMed:14557547, ECO:0000269|PubMed:14756778,
ECO:0000269|PubMed:16030141, ECO:0000269|PubMed:16368961}.
-!- 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 quite important in this effect
(PubMed:14557547, PubMed:14756778, PubMed:16368961).
{ECO:0000269|PubMed:14557547, ECO:0000269|PubMed:14756778,
ECO:0000269|PubMed:16368961}.
-!- 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}.
-!- SIMILARITY: Belongs to the WXG100 family. CFP-10 subfamily.
{ECO:0000305|PubMed:19876390}.
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EMBL; AF004671; AAC83445.1; -; Genomic_DNA.
EMBL; AF419854; AAL14999.1; -; Genomic_DNA.
EMBL; AL123456; CCP46703.1; -; Genomic_DNA.
PIR; H70802; H70802.
RefSeq; NP_218391.1; NC_000962.3.
RefSeq; WP_003399940.1; NZ_KK339374.1.
PDB; 1WA8; NMR; -; A=2-100.
PDB; 3FAV; X-ray; 2.15 A; A/C=1-100.
PDBsum; 1WA8; -.
PDBsum; 3FAV; -.
ProteinModelPortal; P9WNK5; -.
SMR; P9WNK5; -.
IntAct; P9WNK5; 13.
STRING; 83332.Rv3874; -.
iPTMnet; P9WNK5; -.
PaxDb; P9WNK5; -.
EnsemblBacteria; CCP46703; CCP46703; Rv3874.
GeneID; 886194; -.
KEGG; mtu:Rv3874; -.
TubercuList; Rv3874; -.
OMA; MVGQAGT; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0046812; F:host cell surface binding; 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; Cell wall; Chaperone; Coiled coil;
Complete proteome; Direct protein sequencing;
Host endoplasmic reticulum; Reference proteome; Secreted; Virulence.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609,
ECO:0000269|PubMed:9846755}.
CHAIN 2 100 ESAT-6-like protein EsxB.
/FTId=PRO_0000167796.
REGION 87 100 Required for ESAT-6/CFP-10 complex to
bind to host macrophage and monocytes.
{ECO:0000269|PubMed:15973432}.
COILED 7 42 {ECO:0000305|PubMed:16048998}.
COILED 49 86 {ECO:0000255,
ECO:0000305|PubMed:16048998}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:21969609}.
MUTAGEN 42 42 Q->P: Abolishes EsxB-EsxA heterodimer
interaction with EccCb1 and EspA,
maintains interaction with EccA2 and
EccE2. {ECO:0000269|PubMed:19854905}.
MUTAGEN 62 62 A->S: Abolishes EsxB-EsxA heterodimer
interaction with EccCb1, weaker
interaction with EspA, maintains
interaction with EccA2 and EccE2.
{ECO:0000269|PubMed:19854905}.
MUTAGEN 94 94 L->A: Abolishes interaction with EccCb1,
but not with EsxA.
{ECO:0000269|PubMed:16973880}.
MUTAGEN 95 95 S->T: Abolishes EsxB-EsxA heterodimer
interaction with EccCb1, maintains
interaction with EspA, EccA2 and EccE2.
{ECO:0000269|PubMed:19854905}.
MUTAGEN 96 96 S->A: No change in stability.
{ECO:0000269|PubMed:16973880}.
MUTAGEN 98 98 M->A: Abolishes interaction with EccCb1,
but not with EsxA. No change in
stability, but loss of secretion.
{ECO:0000269|PubMed:16973880}.
MUTAGEN 99 99 G->A: Abolishes interaction with EccCb1,
but not with EsxA.
{ECO:0000269|PubMed:16973880}.
MUTAGEN 100 100 F->A: Abolishes interaction with EccCb1,
but not with EsxA. No change in
stability, but loss of secretion.
{ECO:0000269|PubMed:16973880}.
HELIX 2 10 {ECO:0000244|PDB:3FAV}.
HELIX 12 37 {ECO:0000244|PDB:3FAV}.
TURN 38 41 {ECO:0000244|PDB:3FAV}.
HELIX 45 83 {ECO:0000244|PDB:3FAV}.
HELIX 85 89 {ECO:0000244|PDB:3FAV}.
SEQUENCE 100 AA; 10794 MW; 285F4FC96F55D194 CRC64;
MAEMKTDAAT LAQEAGNFER ISGDLKTQID QVESTAGSLQ GQWRGAAGTA AQAAVVRFQE
AANKQKQELD EISTNIRQAG VQYSRADEEQ QQALSSQMGF


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