ESPJ_MYCTU
ID ESPJ_MYCTU Reviewed; 280 AA.
AC P9WJC3; L0TFI6; O69742; Q7D4P1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=ESX-1 secretion-associated protein EspJ {ECO:0000305};
DE AltName: Full=TB27.4 {ECO:0000303|PubMed:14632649};
GN Name=espJ {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv3878;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IMMUNE RESPONSE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14632649; DOI=10.1111/j.1365-2567.2003.01763.x;
RA Agger E.M., Brock I., Okkels L.M., Arend S.M., Aagaard C.S., Weldingh K.N.,
RA Andersen P.;
RT "Human T-cell responses to the RD1-encoded protein TB27.4 (Rv3878) from
RT Mycobacterium tuberculosis.";
RL Immunology 110:507-512(2003).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=16368961; DOI=10.1128/iai.74.1.88-98.2006;
RA Brodin P., Majlessi L., Marsollier L., de Jonge M.I., Bottai D.,
RA Demangel C., Hinds J., Neyrolles O., Butcher P.D., Leclerc C., Cole S.T.,
RA Brosch R.;
RT "Dissection of ESAT-6 system 1 of Mycobacterium tuberculosis and impact on
RT immunogenicity and virulence.";
RL Infect. Immun. 74:88-98(2006).
RN [4]
RP GENE NAME.
RX PubMed=19876390; DOI=10.1371/journal.ppat.1000507;
RA Bitter W., Houben E.N., Bottai D., Brodin P., Brown E.J., Cox J.S.,
RA Derbyshire K., Fortune S.M., Gao L.Y., Liu J., Gey van Pittius N.C.,
RA Pym A.S., Rubin E.J., Sherman D.R., Cole S.T., Brosch R.;
RT "Systematic genetic nomenclature for type VII secretion systems.";
RL PLoS Pathog. 5:E1000507-E1000507(2009).
RN [5]
RP SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19854905; DOI=10.1128/jb.01032-09;
RA Callahan B., Nguyen K., Collins A., Valdes K., Caplow M., Crossman D.K.,
RA Steyn A.J., Eisele L., Derbyshire K.M.;
RT "Conservation of structure and protein-protein interactions mediated by the
RT secreted mycobacterial proteins EsxA, EsxB, and EspA.";
RL J. Bacteriol. 192:326-335(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION AT SER-70,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-70.
RX PubMed=26228622; DOI=10.1038/srep12717;
RA Singh P.K., Saxena R., Tiwari S., Singh D.K., Singh S.K., Kumari R.,
RA Srivastava K.K.;
RT "RD-1 encoded EspJ protein gets phosphorylated prior to affect the growth
RT and intracellular survival of mycobacteria.";
RL Sci. Rep. 5:12717-12717(2015).
CC -!- FUNCTION: Could be involved in regulation of growth and intracellular
CC survival. {ECO:0000269|PubMed:26228622}.
CC -!- SUBUNIT: Residues 76-280 interact with EsxB and an artificial EsxB-EsxA
CC heterodimer (PubMed:19854905). {ECO:0000269|PubMed:19854905}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26228622}.
CC -!- INDUCTION: Induced during stationary phase.
CC {ECO:0000269|PubMed:26228622}.
CC -!- PTM: Phosphorylated at Ser-70. {ECO:0000269|PubMed:26228622}.
CC -!- DISRUPTION PHENOTYPE: Inactivation does not abolish EsxA (ESAT-6)
CC secretion, EsxA-specific immunogenicity and enhanced virulence
CC (PubMed:16368961). Deletion mutants multiply more efficiently compared
CC to wild-type strains (PubMed:26228622). {ECO:0000269|PubMed:16368961,
CC ECO:0000269|PubMed:26228622}.
CC -!- MISCELLANEOUS: Elicits a prominent immune response in human
CC tuberculosis patients. Contains several epitopes, particularly in the
CC C-terminal region. {ECO:0000269|PubMed:14632649}.
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DR EMBL; AL123456; CCP46707.1; -; Genomic_DNA.
DR PIR; D70803; D70803.
DR RefSeq; NP_218395.1; NC_000962.3.
DR RefSeq; WP_003901751.1; NZ_NVQJ01000086.1.
DR AlphaFoldDB; P9WJC3; -.
DR SMR; P9WJC3; -.
DR IntAct; P9WJC3; 1.
DR STRING; 83332.Rv3878; -.
DR iPTMnet; P9WJC3; -.
DR PaxDb; P9WJC3; -.
DR DNASU; 886198; -.
DR GeneID; 886198; -.
DR KEGG; mtu:Rv3878; -.
DR TubercuList; Rv3878; -.
DR eggNOG; ENOG50320XY; Bacteria.
DR OMA; QMAQMPM; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Secreted; Virulence.
FT CHAIN 1..280
FT /note="ESX-1 secretion-associated protein EspJ"
FT /id="PRO_0000394148"
FT REGION 167..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26228622"
FT MUTAGEN 70
FT /note="S->A: Lack of phosphorylation. Increases the growth
FT of mycobacteria."
FT /evidence="ECO:0000269|PubMed:26228622"
SQ SEQUENCE 280 AA; 27395 MW; 70B209E9EE7CADB5 CRC64;
MAEPLAVDPT GLSAAAAKLA GLVFPQPPAP IAVSGTDSVV AAINETMPSI ESLVSDGLPG
VKAALTRTAS NMNAAADVYA KTDQSLGTSL SQYAFGSSGE GLAGVASVGG QPSQATQLLS
TPVSQVTTQL GETAAELAPR VVATVPQLVQ LAPHAVQMSQ NASPIAQTIS QTAQQAAQSA
QGGSGPMPAQ LASAEKPATE QAEPVHEVTN DDQGDQGDVQ PAEVVAAARD EGAGASPGQQ
PGGGVPAQAM DTGAGARPAA SPLAAPVDPS TPAPSTTTTL
