ID   DNAK_FRATU              Reviewed;         642 AA.
AC   P48205;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Francisella tularensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=263;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7590305; DOI=10.1016/0378-1119(95)00489-s;
RA   Zuber M., Hoover T.A., Dertzbaugh M.T., Court D.L.;
RT   "Analysis of the DnaK molecular chaperone system of Francisella
RT   tularensis.";
RL   Gene 164:149-152(1995).
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; L43367; AAA69561.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48205; -.
DR   SMR; P48205; -.
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; 1.
DR   Pfam; PF00012; HSP70; 1.
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..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078464"
FT   REGION          609..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..642
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         201
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   642 AA;  69208 MW;  7DCFA7B4714E96EA CRC64;
     MGKIIGIDLG TTNSCLAIMD GKTAKVIENA EGHRTTPSVV AYTDSGEILV GQAAKRQAVT
     NPDNTFFAIK RLIGRKYDDK AVQEDIKKKV PYAVIKADNG DAWVATKEGK KMAPPQVSAE
     VLRKMKKTAE DYLGEPVTEA VITVPAYFND SQRQATKDAG KIAGLEVKRI INEPTAAALA
     YGVDSKKGEQ TVAVYDLGGG TFDISIIEIS DVDGDNQIEV LSTNGDTFLG GEDFDLALMN
     YLIDEFKKEQ GIDLHNDKLA LQRVREAAEK AKVELSPAQQ TDVNLPYITA DATGPKHLNI
     KVTRAKFESL VSDLVMRSLE PCKKALEDAG LSKSDITEVL LVGGQTRMPL VQEKVKEFFG
     KEPRKDVNPD EAVAVGAAIQ GGVLAGDVKD VLLLDVTPLS LGIETMGGVM TKLIERNTTI
     PTKKSQVFST AEDNQPAVTI HVLQGEREMA SANKSLGRFD LADIPPAPRG MPQIEVTFDI
     DANGILNVSA KDKATGKEQN IVIKSSSGLS EEDIEKMVQD AEANAEADKK FHDLVTARNT
     ADNLIHSSRK AIQELGDKVT AAEKEKIEEA CKELEAATKG DDKQAIEAKT KALEEAFAPI
     AQKAYAEQAQ AAGAQGGAKA EEPKKEEDVV DADFEDVEDD KK