ESXG_MYCTU
ID ESXG_MYCTU Reviewed; 97 AA.
AC O53692; F2GM91; I6Y3F0; Q7DA34;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=ESAT-6-like protein EsxG {ECO:0000305};
DE AltName: Full=Conserved protein TB9.8 {ECO:0000305};
GN Name=esxG {ECO:0000303|PubMed:15336430, ECO:0000303|PubMed:19876390};
GN OrderedLocusNames=Rv0287 {ECO:0000312|EMBL:CCP43017.1};
GN ORFNames=LH57_01570 {ECO:0000312|EMBL:AIR13010.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH ESXH.
RX PubMed=15336430; DOI=10.1111/j.1574-6968.2004.tb09764.x;
RA Lightbody K.L., Renshaw P.S., Collins M.L., Wright R.L., Hunt D.M.,
RA Gordon S.V., Hewinson R.G., Buxton R.S., Williamson R.A., Carr M.D.;
RT "Characterisation of complex formation between members of the Mycobacterium
RT tuberculosis complex CFP-10/ESAT-6 protein family: towards an understanding
RT of the rules governing complex formation and thereby functional
RT flexibility.";
RL FEMS Microbiol. Lett. 238:255-262(2004).
RN [4]
RP INTERACTION WITH ESXH.
RX PubMed=18430736; DOI=10.1074/jbc.m800123200;
RA Lightbody K.L., Ilghari D., Waters L.C., Carey G., Bailey M.A.,
RA Williamson R.A., Renshaw P.S., Carr M.D.;
RT "Molecular features governing the stability and specificity of functional
RT complex formation by Mycobacterium tuberculosis CFP-10/ESAT-6 family
RT proteins.";
RL J. Biol. Chem. 283:17681-17690(2008).
RN [5]
RP NOMENCLATURE.
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 [6]
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 [7]
RP SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20085764; DOI=10.1016/j.febslet.2009.12.057;
RA Poulsen C., Holton S., Geerlof A., Wilmanns M., Song Y.H.;
RT "Stoichiometric protein complex formation and over-expression using the
RT prokaryotic native operon structure.";
RL FEBS Lett. 584:669-674(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP FUNCTION IN VIRULENCE, AND INTERACTION WITH ESXH.
RC STRAIN=H37Rv;
RX PubMed=24204276; DOI=10.1371/journal.ppat.1003734;
RA Mehra A., Zahra A., Thompson V., Sirisaengtaksin N., Wells A., Porto M.,
RA Koester S., Penberthy K., Kubota Y., Dricot A., Rogan D., Vidal M.,
RA Hill D.E., Bean A.J., Philips J.A.;
RT "Mycobacterium tuberculosis type VII secreted effector EsxH targets host
RT ESCRT to impair trafficking.";
RL PLoS Pathog. 9:E1003734-E1003734(2013).
RN [10]
RP STRUCTURE BY NMR, INTERACTION WITH ESXH, AND SUBCELLULAR LOCATION.
RX PubMed=21730061; DOI=10.1074/jbc.m111.248732;
RA Ilghari D., Lightbody K.L., Veverka V., Waters L.C., Muskett F.W.,
RA Renshaw P.S., Carr M.D.;
RT "Solution structure of the Mycobacterium tuberculosis EsxG.EsxH complex:
RT functional implications and comparisons with other M. tuberculosis Esx
RT family complexes.";
RL J. Biol. Chem. 286:29993-30002(2011).
CC -!- FUNCTION: EsxG, in complex with EsxH, disrupts ESCRT function and
CC impairs host phagosome maturation, thereby promoting intracellular
CC bacterial growth. The complex acts by interacting, via EsxH, with the
CC host hepatocyte growth factor-regulated tyrosine kinase substrate
CC (HGS/HRS), a component of the ESCRT machinery. EsxG stabilizes EsxH in
CC the host cytosol. {ECO:0000269|PubMed:24204276}.
CC -!- SUBUNIT: Forms a tight 1:1 complex with EsxH.
CC {ECO:0000269|PubMed:15336430, ECO:0000269|PubMed:18430736,
CC ECO:0000269|PubMed:19854905, ECO:0000269|PubMed:20085764,
CC ECO:0000269|PubMed:21730061, ECO:0000269|PubMed:24204276}.
CC -!- INTERACTION:
CC O53692; P9WNK3: esxH; NbExp=4; IntAct=EBI-6409586, EBI-6409599;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21730061}.
CC Note=Secreted via the ESX-3 / type VII secretion system (T7SS).
CC {ECO:0000305|PubMed:21730061}.
CC -!- MISCELLANEOUS: To improve expression in E.coli the proteins were cloned
CC as a single protein in the order esxH-esxG with a cleavable thrombin
CC tag (PubMed:19854905). {ECO:0000269|PubMed:19854905}.
CC -!- SIMILARITY: Belongs to the WXG100 family. CFP-10 subfamily.
CC {ECO:0000305|PubMed:19876390}.
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DR EMBL; CP009480; AIR13010.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43017.1; -; Genomic_DNA.
DR RefSeq; NP_214801.1; NC_000962.3.
DR RefSeq; WP_003401503.1; NZ_NVQJ01000026.1.
DR PDB; 2KG7; NMR; -; A=1-97.
DR PDBsum; 2KG7; -.
DR AlphaFoldDB; O53692; -.
DR SMR; O53692; -.
DR IntAct; O53692; 1.
DR MINT; O53692; -.
DR STRING; 83332.Rv0287; -.
DR iPTMnet; O53692; -.
DR PaxDb; O53692; -.
DR PRIDE; O53692; -.
DR DNASU; 886604; -.
DR GeneID; 45424261; -.
DR GeneID; 886604; -.
DR KEGG; mtu:Rv0287; -.
DR PATRIC; fig|83332.111.peg.323; -.
DR TubercuList; Rv0287; -.
DR eggNOG; ENOG5030NJS; Bacteria.
DR HOGENOM; CLU_161983_0_0_11; -.
DR PhylomeDB; O53692; -.
DR Reactome; R-HSA-9635644; Inhibition of membrane repair.
DR Reactome; R-HSA-9636383; Prevention of phagosomal-lysosomal fusion.
DR EvolutionaryTrace; O53692; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
DR GO; GO:0097013; C:phagocytic vesicle lumen; TAS:Reactome.
DR InterPro; IPR036689; ESAT-6-like_sf.
DR InterPro; IPR010310; T7SS_ESAT-6-like.
DR Pfam; PF06013; WXG100; 1.
DR SUPFAM; SSF140453; SSF140453; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Reference proteome; Secreted; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..97
FT /note="ESAT-6-like protein EsxG"
FT /id="PRO_0000434997"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:2KG7"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2KG7"
FT HELIX 17..39
FT /evidence="ECO:0007829|PDB:2KG7"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2KG7"
FT HELIX 49..76
FT /evidence="ECO:0007829|PDB:2KG7"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2KG7"
SQ SEQUENCE 97 AA; 9778 MW; 927527DA610A1637 CRC64;
MSLLDAHIPQ LVASQSAFAA KAGLMRHTIG QAEQAAMSAQ AFHQGESSAA FQAAHARFVA
AAAKVNTLLD VAQANLGEAA GTYVAADAAA ASTYTGF
