ID   ESPE_MYCTU              Reviewed;         402 AA.
AC   P9WJD3; L0TDS9; P96213; Q7D4P9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=ESX-1 secretion-associated protein EspE {ECO:0000305};
GN   Name=espE; OrderedLocusNames=Rv3864;
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.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=14756778; DOI=10.1046/j.1365-2958.2003.03844.x;
RA   Guinn K.M., Hickey M.J., Mathur S.K., Zakel K.L., Grotzke J.E.,
RA   Lewinsohn D.M., Smith S., Sherman D.R.;
RT   "Individual RD1-region genes are required for export of ESAT-6/CFP-10 and
RT   for virulence of Mycobacterium tuberculosis.";
RL   Mol. Microbiol. 51:359-370(2004).
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   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   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=H37Rv;
RX   PubMed=22233444; DOI=10.1111/j.1365-2958.2011.07958.x;
RA   Wirth S.E., Krywy J.A., Aldridge B.B., Fortune S.M., Fernandez-Suarez M.,
RA   Gray T.A., Derbyshire K.M.;
RT   "Polar assembly and scaffolding proteins of the virulence-associated ESX-1
RT   secretory apparatus in mycobacteria.";
RL   Mol. Microbiol. 83:654-664(2012).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000255}. Note=Localizes at or near the cell pole
CC       in (on average) 1 discrete spot upon overexpression in M.smegmatis
CC       (PubMed:22233444). {ECO:0000269|PubMed:22233444}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation does not abolish EsxA (ESAT-6)
CC       secretion, EsxA-specific immunogenicity and enhanced virulence.
CC       {ECO:0000269|PubMed:14756778, ECO:0000269|PubMed:16368961}.
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DR   EMBL; AL123456; CCP46693.1; -; Genomic_DNA.
DR   PIR; E70656; E70656.
DR   RefSeq; NP_218381.1; NC_000962.3.
DR   RefSeq; WP_003899736.1; NZ_KK339374.1.
DR   AlphaFoldDB; P9WJD3; -.
DR   STRING; 83332.Rv3864; -.
DR   PaxDb; P9WJD3; -.
DR   DNASU; 886185; -.
DR   GeneID; 886185; -.
DR   KEGG; mtu:Rv3864; -.
DR   TubercuList; Rv3864; -.
DR   eggNOG; COG3266; Bacteria.
DR   OMA; SGSAMCK; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR   InterPro; IPR043796; ESX-1_EspA/EspE-like.
DR   Pfam; PF18879; EspA_EspE; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..402
FT                   /note="ESX-1 secretion-associated protein EspE"
FT                   /id="PRO_0000393950"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          345..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  42069 MW;  B400E0E22D482765 CRC64;
     MASGSGLCKT TSNFIWGQLL LLGEGIPDPG DIFNTGSSLF KQISDKMGLA IPGTNWIGQA
     AEAYLNQNIA QQLRAQVMGD LDKLTGNMIS NQAKYVSDTR DVLRAMKKMI DGVYKVCKGL
     EKIPLLGHLW SWELAIPMSG IAMAVVGGAL LYLTIMTLMN ATNLRGILGR LIEMLTTLPK
     FPGLPGLPSL PDIIDGLWPP KLPDIPIPGL PDIPGLPDFK WPPTPGSPLF PDLPSFPGFP
     GFPEFPAIPG FPALPGLPSI PNLFPGLPGL GDLLPGVGDL GKLPTWTELA ALPDFLGGFA
     GLPSLGFGNL LSFASLPTVG QVTATMGQLQ QLVAAGGGPS QLASMGSQQA QLISSQAQQG
     GQQHATLVSD KKEDEEGVAE AERAPIDAGT AASQRGQEGT VL