ID   DNAK_MYCMS              Reviewed;         591 AA.
AC   Q6MT06;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=MSC_0610;
OS   Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT   PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL   Genome Res. 14:221-227(2004).
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; BX293980; CAE77232.1; -; Genomic_DNA.
DR   RefSeq; NP_975590.1; NC_005364.2.
DR   AlphaFoldDB; Q6MT06; -.
DR   SMR; Q6MT06; -.
DR   STRING; 272632.MSC_0610; -.
DR   PRIDE; Q6MT06; -.
DR   EnsemblBacteria; CAE77232; CAE77232; MSC_0610.
DR   KEGG; mmy:MSC_0610; -.
DR   PATRIC; fig|272632.4.peg.657; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_14; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001016; 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; 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; 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; 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   Reference proteome; Stress response.
FT   CHAIN           1..591
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225982"
FT   REGION          568..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..591
FT                   /note="Polar residues"
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   591 AA;  63954 MW;  030C0FF381F66726 CRC64;
     MAKEKIIGID LGTTNSVVSV IEGGQPIILE NPEGQRTTPS VVAFKNSDII VGGAAKRQAV
     TNPNVVQSIK SKMGTTSKVN LEGKDYSPEQ ISAEILRYMK NYAEAKLGQK VTKAVITVPA
     YFNDAQRKAT KDAGTIAGLQ VERIINEPTA AALAYGLDKQ DKEETILVYD LGGGTFDVSI
     LAIGGGSFDV IATSGNNKLG GDNFDEEIIK WLLGKIKAEY NIDLSKEKMA LQRLKDEAEK
     AKINLSSQLE VEINLPFIAM NESGPISFAT TLTRSEFNKI TKHLVDLTIQ PVKDALSAAK
     KTPSEINEVL LVGGSTRIPA VQELVKSLLN KEPNRSINPD EVVAMGAAVQ GGVLAGEVTD
     ILLLDVTPLS LGIETMGGVM TKLIERNTTI PAKRTQIFST ATDNQPAVDI NVLQGERAMA
     ADNKSLGQFQ LTGIQPAPRG VPQIEVTFEI DANGIVSVSA KDKNTNEEKT ITISNSGNLS
     EAEVERMIKE AQENAANDEV KKKNIELKNK AENYINIIEN SLLQAGDKIS AEQKEQSQKM
     VDEIKELVKN ENYEALEQKM AELEQAMAQA AEFANKQNES DPNNNSSEQN N