ID   DNAK_MYCUA              Reviewed;         622 AA.
AC   A0PLQ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=MUL_0593;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; CP000325; ABL03270.1; -; Genomic_DNA.
DR   RefSeq; WP_011738895.1; NC_008611.1.
DR   AlphaFoldDB; A0PLQ1; -.
DR   SMR; A0PLQ1; -.
DR   STRING; 362242.MUL_0593; -.
DR   PRIDE; A0PLQ1; -.
DR   EnsemblBacteria; ABL03270; ABL03270; MUL_0593.
DR   KEGG; mul:MUL_0593; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000765; 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   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..622
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059612"
FT   REGION          589..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   622 AA;  66402 MW;  1183F83B35EADEEA CRC64;
     MARAVGIDLG TTNSVVAVLE GGDPVVVANS EGSRTTPSVV AFARNGEVLV GQPAKNQAVT
     NVERTMRSVK RHMGGDWSIE IDDKKYTTPE ISARVLMKLK RDAEAYLGED IADAVITVPA
     YFNDAQRQAT KDAGQIAGLN VLRIVNEPTA AALAYGLDKG EKDQTILVFD LGGGTFDVSL
     LEIGEGVVEV RATSGDNHLG GDDWDDRVVE WLVDKFKGTS GIDLTKDKMA MQRLREAAEK
     AKIELSSSQS TSINLPYITV DADKNPLFLD EQLTRAEFQR ITQDLLDRTR KPFQSVIADT
     GISVSDIDHV VLVGGSTRMP AVTELVKELT GGKEPNKGVN PDEVVAVGAA LQAGVLKGEV
     KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTADDNQPSV QIQVYQGERE
     IAAHNKLLGS FELTGIPPAP RGVSQIEVTF DIDANGIVHV TAKDKGTGKE NTIRIQEGSG
     LSKDEIDRMI KDAEAHAAED HKRREEADVR NQAETLVYQT EKFVKEQREA EGGSKVPEDT
     LNKVDAAVAE AKSALAGTDI AAIKSAMEKL GQESQALGQA IYEATQADAA AAGAPGGQPG
     GAEPGADDVV DAEVVDDDQE SK