ID   ESPK_MYCTU              Reviewed;         729 AA.
AC   P9WJC1; 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 32.
DE   RecName: Full=ESX-1 secretion-associated protein EspK {ECO:0000305};
GN   Name=espK {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv3879c;
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   FUNCTION, INTERACTION WITH ESPB AND ECCCB1, AND SUBCELLULAR LOCATION.
RX   PubMed=17676952; DOI=10.1371/journal.ppat.0030105;
RA   McLaughlin B., Chon J.S., MacGurn J.A., Carlsson F., Cheng T.L., Cox J.S.,
RA   Brown E.J.;
RT   "A mycobacterium ESX-1-secreted virulence factor with unique requirements
RT   for export.";
RL   PLoS Pathog. 3:E105-E105(2007).
RN   [4]
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   [5]
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: May act as a chaperone that facilitates EspB secretion
CC       through an interaction with EccCb1. {ECO:0000269|PubMed:17676952}.
CC   -!- SUBUNIT: Interacts with EspB and EccCb1. {ECO:0000269|PubMed:17676952}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17676952}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation does not abolish EsxA (ESAT-6)
CC       secretion, EsxA-specific immunogenicity and enhanced virulence.
CC       {ECO:0000269|PubMed:16368961}.
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DR   EMBL; AL123456; CCP46708.1; -; Genomic_DNA.
DR   PIR; E70803; E70803.
DR   RefSeq; NP_218396.1; NC_000962.3.
DR   RefSeq; WP_010886183.1; NZ_NVQJ01000086.1.
DR   AlphaFoldDB; P9WJC1; -.
DR   SASBDB; P9WJC1; -.
DR   SMR; P9WJC1; -.
DR   STRING; 83332.Rv3879c; -.
DR   PaxDb; P9WJC1; -.
DR   GeneID; 886212; -.
DR   KEGG; mtu:Rv3879c; -.
DR   TubercuList; Rv3879c; -.
DR   eggNOG; COG4932; Bacteria.
DR   OMA; QHLAVIM; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   InterPro; IPR036689; ESAT-6-like_sf.
DR   SUPFAM; SSF140453; SSF140453; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..729
FT                   /note="ESX-1 secretion-associated protein EspK"
FT                   /id="PRO_0000394149"
FT   REGION          175..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..324
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   729 AA;  74492 MW;  2CD7EDA17FC4CE9E CRC64;
     MSITRPTGSY ARQMLDPGGW VEADEDTFYD RAQEYSQVLQ RVTDVLDTCR QQKGHVFEGG
     LWSGGAANAA NGALGANINQ LMTLQDYLAT VITWHRHIAG LIEQAKSDIG NNVDGAQREI
     DILENDPSLD ADERHTAINS LVTATHGANV SLVAETAERV LESKNWKPPK NALEDLLQQK
     SPPPPDVPTL VVPSPGTPGT PGTPITPGTP ITPGTPITPI PGAPVTPITP TPGTPVTPVT
     PGKPVTPVTP VKPGTPGEPT PITPVTPPVA PATPATPATP VTPAPAPHPQ PAPAPAPSPG
     PQPVTPATPG PSGPATPGTP GGEPAPHVKP AALAEQPGVP GQHAGGGTQS GPAHADESAA
     SVTPAAASGV PGARAAAAAP SGTAVGAGAR SSVGTAAASG AGSHAATGRA PVATSDKAAA
     PSTRAASART APPARPPSTD HIDKPDRSES ADDGTPVSMI PVSAARAARD AATAAASARQ
     RGRGDALRLA RRIAAALNAS DNNAGDYGFF WITAVTTDGS IVVANSYGLA YIPDGMELPN
     KVYLASADHA IPVDEIARCA TYPVLAVQAW AAFHDMTLRA VIGTAEQLAS SDPGVAKIVL
     EPDDIPESGK MTGRSRLEVV DPSAAAQLAD TTDQRLLDLL PPAPVDVNPP GDERHMLWFE
     LMKPMTSTAT GREAAHLRAF RAYAAHSQEI ALHQAHTATD AAVQRVAVAD WLYWQYVTGL
     LDRALAAAC