ID   ESPL_MYCTU              Reviewed;         115 AA.
AC   P9WJB9; L0TE21; O69744; Q7D4P0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=ESX-1 secretion-associated protein EspL {ECO:0000305};
GN   Name=espL {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv3880c;
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   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   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Beijing GC1237;
RX   PubMed=20844580; DOI=10.1371/journal.ppat.1001100;
RA   Brodin P., Poquet Y., Levillain F., Peguillet I., Larrouy-Maumus G.,
RA   Gilleron M., Ewann F., Christophe T., Fenistein D., Jang J., Jang M.S.,
RA   Park S.J., Rauzier J., Carralot J.P., Shrimpton R., Genovesio A.,
RA   Gonzalo-Asensio J.A., Puzo G., Martin C., Brosch R., Stewart G.R.,
RA   Gicquel B., Neyrolles O.;
RT   "High content phenotypic cell-based visual screen identifies Mycobacterium
RT   tuberculosis acyltrehalose-containing glycolipids involved in phagosome
RT   remodeling.";
RL   PLoS Pathog. 6:E1001100-E1001100(2010).
RN   [4]
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).
CC   -!- FUNCTION: Probably plays a role in host phagosome maturation arrest
CC       (PubMed:20844580). {ECO:0000305|PubMed:20844580}.
CC   -!- INTERACTION:
CC       P9WJB9; P9WJD5: espD; NbExp=2; IntAct=EBI-25767670, EBI-26358082;
CC   -!- DISRUPTION PHENOTYPE: Grows normally in liquid culture, traffics into
CC       host (human and mouse) acidified compartments early after phagocytosis,
CC       suggesting it no longer arrests phagosome maturation as well as wild-
CC       type, impaired growth in mouse macrophages (PubMed:20844580).
CC       {ECO:0000269|PubMed:20844580}.
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DR   EMBL; AL123456; CCP46709.1; -; Genomic_DNA.
DR   PIR; F70803; F70803.
DR   RefSeq; NP_218397.1; NC_000962.3.
DR   RefSeq; WP_003399988.1; NZ_NVQJ01000086.1.
DR   AlphaFoldDB; P9WJB9; -.
DR   SMR; P9WJB9; -.
DR   BioGRID; 4355680; 1.
DR   IntAct; P9WJB9; 16.
DR   MINT; P9WJB9; -.
DR   STRING; 83332.Rv3880c; -.
DR   iPTMnet; P9WJB9; -.
DR   PaxDb; P9WJB9; -.
DR   GeneID; 45427883; -.
DR   GeneID; 886205; -.
DR   KEGG; mtu:Rv3880c; -.
DR   PATRIC; fig|83332.111.peg.4320; -.
DR   TubercuList; Rv3880c; -.
DR   eggNOG; ENOG5031T2G; Bacteria.
DR   OMA; TLNGHHW; -.
DR   PHI-base; PHI:8763; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0052170; P:suppression by symbiont of host innate immune response; IDA:MTBBASE.
DR   Gene3D; 3.30.1310.10; -; 1.
DR   InterPro; IPR036894; YbaB-like_sf.
DR   InterPro; IPR004401; YbaB/EbfC.
DR   Pfam; PF02575; YbaB_DNA_bd; 1.
DR   SUPFAM; SSF82607; SSF82607; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   CHAIN           2..115
FT                   /note="ESX-1 secretion-associated protein EspL"
FT                   /id="PRO_0000394150"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
SQ   SEQUENCE   115 AA;  12200 MW;  21F649625106A128 CRC64;
     MSMDELDPHV ARALTLAARF QSALDGTLNQ MNNGSFRATD EAETVEVTIN GHQWLTGLRI
     EDGLLKKLGA EAVAQRVNEA LHNAQAAASA YNDAAGEQLT AALSAMSRAM NEGMA