ID   DNAK_METSS              Reviewed;         641 AA.
AC   Q9ZFC6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Methylovorus sp. (strain SS1 / DSM 11726).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylovorus; unclassified Methylovorus.
OX   NCBI_TaxID=81683;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Eom C.Y., Kim Y.M.;
RT   "grpE, dnaK, and dnaJ genes of Methylovorus sp. strain SS1 DSM11726.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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; AF106835; AAC95378.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZFC6; -.
DR   SMR; Q9ZFC6; -.
DR   PRIDE; Q9ZFC6; -.
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..641
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078486"
FT   REGION          602..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   641 AA;  69765 MW;  7DFA5EBE144825CB CRC64;
     MAKIIGIDLG TTNSCVAVME GGKPRVIENA EGTRTTPSIV AYQDDGEILA GAPAKRQAVT
     NPKNTLYAVK RLIGRRFEEK EVQKDIGLMP YTITKADNGD AWVEVRGQKM APPPNSAEVL
     RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
     LDKQEGDRKI AVYDLGGGTF DISIIEIAEI DGEHQFEVLS TNGDTFLGGE DFDNRLIDFL
     ADEFKKEKRL DLRNDLLAKQ RLKEAAEKAK IELSSAQQTE VNLPYITADA TGPKHLVVKI
     TRTKFESLVE DLIERSIKPC EVALKDAGVK PSDIQDVILV GGQTRMPKVQ EKVKEFFGKE
     PRKDVNPDEA VAVGAAIQGG VLQGDVKDVL LLDVTPLSLG IETLGGVMTK LIKKNTTIPT
     KASQVFSTAE DNQNAVTIQV LQGEREMAAG NKSLGQFNLS DIPPAPRGMP QIEVTFDIDA
     NAILHVSAKD KATGKENKIT IKANSGLSEE EIKRMEEDAA AYADEDRKLR ELVDARNSAD
     GMVHSVKKSL SEHGDKLEAG EKEKIEAAIK DVEDAIKGDD KEAIEAKTNA LMEASQKLGE
     KVYAEQQAQQ GGAEEAQPQG EKTVDADVVD AEFEEVKDDK K