ID   DNAK_MYCLE              Reviewed;         620 AA.
AC   P19993;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=70 kDa antigen;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=ML2496;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2051024;
RA   McKenzie K.R., Adams E., Britton W.J., Garsia R.J., Basten A.;
RT   "Sequence and immunogenicity of the 70-kDa heat shock protein of
RT   Mycobacterium leprae.";
RL   J. Immunol. 147:312-319(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 277-620.
RX   PubMed=2491836; DOI=10.1128/iai.57.1.204-212.1989;
RA   Garsia R.J., Hellqvist L., Booth R.J., Radford A.J., Britton W.J.,
RA   Astbury L., Trent R.J., Basten A.;
RT   "Homology of the 70-kilodalton antigens from Mycobacterium leprae and
RT   Mycobacterium bovis with the Mycobacterium tuberculosis 71-kilodalton
RT   antigen and with the conserved heat shock protein 70 of eucaryotes.";
RL   Infect. Immun. 57:204-212(1989).
RN   [4]
RP   PHOSPHORYLATION AT THR-175.
RX   PubMed=9748655; DOI=10.1016/s0167-4838(98)00156-3;
RA   Peake P., Winter N., Britton W.;
RT   "Phosphorylation of Mycobacterium leprae heat-shock 70 protein at threonine
RT   175 alters its substrate binding characteristics.";
RL   Biochim. Biophys. Acta 1387:387-394(1998).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; M95576; AAA25362.1; -; Genomic_DNA.
DR   EMBL; AL583925; CAC32013.1; -; Genomic_DNA.
DR   PIR; E87221; E87221.
DR   RefSeq; NP_302613.1; NC_002677.1.
DR   RefSeq; WP_010908932.1; NC_002677.1.
DR   AlphaFoldDB; P19993; -.
DR   SMR; P19993; -.
DR   STRING; 272631.ML2496; -.
DR   iPTMnet; P19993; -.
DR   EnsemblBacteria; CAC32013; CAC32013; CAC32013.
DR   KEGG; mle:ML2496; -.
DR   PATRIC; fig|272631.5.peg.4791; -.
DR   Leproma; ML2496; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 2.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..620
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078493"
FT   REGION          588..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:9748655"
FT   CONFLICT        370
FT                   /note="P -> PP (in Ref. 1; AAA25362)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        608..619
FT                   /note="VDAEVVDDERES -> LTRRWSTTNGSP (in Ref. 1 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   620 AA;  66679 MW;  AFE89A7CD3B80D98 CRC64;
     MARAVGIDLG TTNSVVSVLE GGDPVVVANS EGSRTTPSTV AFARNGEVLV GQPAKNQAVT
     NVDRTIRSVK RHMGSDWSIE IDGKKYTAQE ISARVLMKLK RDAEAYLGED ITDAVITTPA
     YFNDAQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLDKG EREQTILVFD LGGGTFDVSL
     LEIGEGVVEV RATSGDNHLG GDDWDDRIVN WLVDKFKGTS GIDLTKDKMA MQRLREAAEK
     AKIELSSSQS TSVNLPYITV DSDKNPLFLD EQLIRAEFQR ITQDLLDRTR QPFQSVVKDA
     GISVSEIDHV VLVGGSTRMP AVTDLVKELT GGKEPNKGVN PDEVVAVGAA LQAGVLKGEV
     KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTADDNQPSV QIQVYQGERE
     IASHNKLLGS FELTGIPPAP RGVPQIEVTF DIDANGIVHV TAKDKGTGKE NTIKIQEGSG
     LSKEEIDRMV KDAEAHAEED RKRREEADVR NQAETLVYQT EKFVKEQRET ENGSRVPEDT
     LNKVEAAVAE AKTALGGTDI SAIKSAMEKL GQDSQALGQA IYEATQAASK VGGEASAPGG
     SNSTDDVVDA EVVDDERESK