ID   DNAK_PRIMG              Reviewed;         605 AA.
AC   P05646;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 116.
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   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3035506; DOI=10.1093/nar/15.9.3923;
RA   Sussman M.D., Setlow P.;
RT   "Nucleotide sequence of a Bacillus megaterium gene homologous to the dnaK
RT   gene of Escherichia coli.";
RL   Nucleic Acids Res. 15:3923-3923(1987).
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; Y00154; CAA68348.1; -; Genomic_DNA.
DR   PIR; I39837; I39837.
DR   RefSeq; WP_013059242.1; NZ_WIPB01000194.1.
DR   AlphaFoldDB; P05646; -.
DR   SMR; P05646; -.
DR   PRIDE; P05646; -.
DR   GeneID; 64145730; -.
DR   OMA; ISIKRHM; -.
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; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..605
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078417"
FT   REGION          578..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   605 AA;  65250 MW;  1CBCC2C4F34A9334 CRC64;
     MSKIIGIDLG TTNSCVAVLE GGEPKVIPNP EGNRTTPSVV AFKNGERQVG EVAKRQAITN
     PNTIISVKRH MGTDHKVEAE GKQYTPQEMS AIILQHLKGY AEEYLGEPVT KAVITVPAYF
     NDAERQATKD AGKIAGLEVE RIINEPTAAA LAYGLEKTDE DQTVLVYDLG GGTFDVSILE
     LGDGVFEVRA TAGDNRLGGD DFDQVIIDYL VAEFKKENGV DLSKDKMALQ RLKDAAEKAK
     KDLSGVTSTQ ISLPFITAGE AGPLHLEVSL SRAKFDELSA GLVERTMAPV RQALKDAGLS
     ASELDKVILV GGSTRIPAVQ DAIKKETGQD PHKGVNPDEV VALGAAIQGG VLTGDVKDVV
     LLDVTPLSLG IETMGGVFTK LIERNTTIPT SKSQVFSTAA DSQTAVDIHV LQGERPMSAD
     NKTLGRFQLT DIPPAPRGVP QIEVSFDIDK NGIVNVRAKD LGTNKEQAIT IKSSTGLSDD
     EIDRMVKEAE ENADADKQRK EEVELRNEAD QLVFTTEKTL KDLEGKVEEA EVTKANEAKD
     ALKAAIEKND LEEIKAKKDE LQEIVQALTV KLYEQAQQAQ QAGEQGAQND DVVDAEFEEV
     NDDKK