ESPG1_MYCTU
ID ESPG1_MYCTU Reviewed; 283 AA.
AC P96210; L0TGZ4;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=ESX-1 secretion-associated protein EspG1 {ECO:0000303|PubMed:21196469};
GN Name=espG1 {ECO:0000303|PubMed:19876390}; Synonyms=snm5;
GN OrderedLocusNames=Rv3866;
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 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 [3]
RP INTERACTION WITH PPE68.
RX PubMed=17433643; DOI=10.1016/j.micres.2006.11.016;
RA Teutschbein J., Schumann G., Mollmann U., Grabley S., Cole S.T., Munder T.;
RT "A protein linkage map of the ESAT-6 secretion system 1 (ESX-1) of
RT Mycobacterium tuberculosis.";
RL Microbiol. Res. 164:253-259(2009).
RN [4]
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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=21196469; DOI=10.1093/infdis/jiq089;
RA Bottai D., Majlessi L., Simeone R., Frigui W., Laurent C., Lenormand P.,
RA Chen J., Rosenkrands I., Huerre M., Leclerc C., Cole S.T., Brosch R.;
RT "ESAT-6 secretion-independent impact of ESX-1 genes espF and espG1 on
RT virulence of Mycobacterium tuberculosis.";
RL J. Infect. Dis. 203:1155-1164(2011).
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).
CC -!- FUNCTION: Specific chaperone for cognate PE/PPE proteins. Plays an
CC important role in preventing aggregation of PE/PPE dimers.
CC {ECO:0000250|UniProtKB:O53943}.
CC -!- SUBUNIT: Interacts specifically with ESX-1-dependent PE/PPE proteins
CC (By similarity). Interacts with PPE68 (PubMed:17433643).
CC {ECO:0000250|UniProtKB:B2HMS9, ECO:0000269|PubMed:17433643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2HSU5}.
CC -!- DISRUPTION PHENOTYPE: Inactivation leads to the attenuation of the
CC recombinant strain, in spite of strong EsxA (ESAT-6) secretion and
CC generation of specific T-cell responses. Mutant has lower amounts of
CC PPE68. {ECO:0000269|PubMed:16368961, ECO:0000269|PubMed:21196469}.
CC -!- SIMILARITY: Belongs to the EspG family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46695.1; -; Genomic_DNA.
DR PIR; G70656; G70656.
DR RefSeq; NP_218383.1; NC_000962.3.
DR RefSeq; WP_003399839.1; NZ_NVQJ01000074.1.
DR AlphaFoldDB; P96210; -.
DR SMR; P96210; -.
DR STRING; 83332.Rv3866; -.
DR PaxDb; P96210; -.
DR DNASU; 886200; -.
DR GeneID; 886200; -.
DR KEGG; mtu:Rv3866; -.
DR TubercuList; Rv3866; -.
DR eggNOG; ENOG502ZNK2; Bacteria.
DR OMA; TLEARWW; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IEP:MTBBASE.
DR InterPro; IPR025734; EspG.
DR Pfam; PF14011; ESX-1_EspG; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..283
FT /note="ESX-1 secretion-associated protein EspG1"
FT /id="PRO_0000394152"
SQ SEQUENCE 283 AA; 30064 MW; 2C883D93E359C606 CRC64;
MTGPSAAGRA GTADNVVGVE VTIDGMLVIA DRLHLVDFPV TLGIRPNIPQ EDLRDIVWEQ
VQRDLTAQGV LDLHGEPQPT VAEMVETLGR PDRTLEGRWW RRDIGGVMVR FVVCRRGDRH
VIAARDGDML VLQLVAPQVG LAGMVTAVLG PAEPANVEPL TGVATELAEC TTASQLTQYG
IAPASARVYA EIVGNPTGWV EIVASQRHPG GTTTQTDAAA GVLDSKLGRL VSLPRRVGGD
LYGSFLPGTQ QNLERALDGL LELLPAGAWL DHTSDHAQAS SRG