ID   ESPK_MYCTO              Reviewed;         723 AA.
AC   P9WJC0; L0TDU5; O69743; Q8VIR7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=ESX-1 secretion-associated protein EspK {ECO:0000250|UniProtKB:P9WJC1};
GN   Name=espK {ECO:0000250|UniProtKB:P9WJC1}; OrderedLocusNames=MT3993;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: May act as a chaperone that facilitates EspB secretion
CC       through an interaction with EccCb1. {ECO:0000250|UniProtKB:P9WJC1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WJC1}.
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DR   EMBL; AE000516; AAK48361.1; -; Genomic_DNA.
DR   PIR; E70803; E70803.
DR   RefSeq; WP_010924728.1; NZ_KK341228.1.
DR   AlphaFoldDB; P9WJC0; -.
DR   SMR; P9WJC0; -.
DR   EnsemblBacteria; AAK48361; AAK48361; MT3993.
DR   KEGG; mtc:MT3993; -.
DR   PATRIC; fig|83331.31.peg.4296; -.
DR   HOGENOM; CLU_021845_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR036689; ESAT-6-like_sf.
DR   SUPFAM; SSF140453; SSF140453; 1.
PE   3: Inferred from homology;
KW   Cytoplasm.
FT   CHAIN           1..723
FT                   /note="ESX-1 secretion-associated protein EspK"
FT                   /id="PRO_0000427856"
FT   REGION          175..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..318
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  73910 MW;  A4B8EC48FC54CF4C CRC64;
     MSITRPTGSY ARQMLDPGGW VEADEDTFYD RAQEYSQVLQ RVTDVLDTCR QQKGHVFEGG
     LWSGGAANAA NGALGANINQ LMTLQDYLAT VITWHRHIAG LIEQAKSDIG NNVDGAQREI
     DILENDPSLD ADERHTAINS LVTATHGANV SLVAETAERV LESKNWKPPK NALEDLLQQK
     SPPPPDVPTL VVPSPGTPGT PGTPITPGTP ITPIPGAPVT PITPTPGTPV TPVTPGKPVT
     PVTPVKPGTP GEPTPITPVT PPVAPATPAT PATPVTPAPA PHPQPAPAPA PSPGPQPVTP
     ATPGPSGPAT PGTPGGEPAP HVKPAALAEQ PGVPGQHAGG GTQSGPAHAD ESAASVTPAA
     ASGVPGARAA AAAPSGTAVG AGARSSVGTA AASGAGSHAA TGRAPVATSD KAAAPSTRAA
     SARTAPPARP PSTDHIDKPD RSESADDGTP VSMIPVSAAR AARDAATAAA SARQRGRGDA
     LRLARRIAAA LNASDNNAGD YGFFWITAVT TDGSIVVANS YGLAYIPDGM ELPNKVYLAS
     ADHAIPVDEI ARCATYPVLA VQAWAAFHDM TLRAVIGTAE QLASSDPGVA KIVLEPDDIP
     ESGKMTGRSR LEVVDPSAAA QLADTTDQRL LDLLPPAPVD VNPPGDERHM LWFELMKPMT
     STATGREAAH LRAFRAYAAH SQEIALHQAH TATDAAVQRV AVADWLYWQY VTGLLDRALA
     AAS