ID   ESPI_MYCTO              Reviewed;         666 AA.
AC   P9WJC4; L0TH05; O69740; Q7D4P3;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=ESX-1 secretion-associated protein EspI {ECO:0000250|UniProtKB:P9WJC5};
GN   Name=espI {ECO:0000250|UniProtKB:P9WJC5}; OrderedLocusNames=MT3990;
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: Required to repress ESX-1-mediated secretion under low ATP
CC       conditions. This function requires the ATP-binding motif.
CC       {ECO:0000250|UniProtKB:P9WJC5}.
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DR   EMBL; AE000516; AAK48358.1; -; Genomic_DNA.
DR   PIR; B70803; B70803.
DR   RefSeq; WP_003909105.1; NC_002755.2.
DR   AlphaFoldDB; P9WJC4; -.
DR   SMR; P9WJC4; -.
DR   EnsemblBacteria; AAK48358; AAK48358; MT3990.
DR   KEGG; mtc:MT3990; -.
DR   HOGENOM; CLU_495924_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01656; CbiA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding.
FT   CHAIN           1..666
FT                   /note="ESX-1 secretion-associated protein EspI"
FT                   /id="PRO_0000427854"
FT   REGION          1..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..50
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..218
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..299
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..368
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         424..431
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P9WJC5"
SQ   SEQUENCE   666 AA;  70645 MW;  752E072FB8B10111 CRC64;
     MAADYDKLFR PHEGMEAPDD MAAQPFFDPS ASFPPAPASA NLPKPNGQTP PPTSDDLSER
     FVSAPPPPPP PPPPPPPTPM PIAAGEPPSP EPAASKPPTP PMPIAGPEPA PPKPPTPPMP
     IAGPEPAPPK PPTPPMPIAG PAPTPTESQL APPRPPTPQT PTGAPQQPES PAPHVPSHGP
     HQPRRTAPAP PWAKMPIGEP PPAPSRPSAS PAEPPTRPAP QHSRRARRGH RYRTDTERNV
     GKVATGPSIQ ARLRAEEASG AQLAPGTEPS PAPLGQPRSY LAPPTRPAPT EPPPSPSPQR
     NSGRRAERRV HPDLAAQHAA AQPDSITAAT TGGRRRKRAA PDLDATQKSL RPAAKGPKVK
     KVKPQKPKAT KPPKVVSQRG WRHWVHALTR INLGLSPDEK YELDLHARVR RNPRGSYQIA
     VVGLKGGAGK TTLTAALGST LAQVRADRIL ALDADPGAGN LADRVGRQSG ATIADVLAEK
     ELSHYNDIRA HTSVNAVNLE VLPAPEYSSA QRALSDADWH FIADPASRFY NLVLADCGAG
     FFDPLTRGVL STVSGVVVVA SVSIDGAQQA SVALDWLRNN GYQDLASRAC VVINHIMPGE
     PNVAVKDLVR HFEQQVQPGR VVVMPWDRHI AAGTEISLDL LDPIYKRKVL ELAAALSDDF
     ERAGRR