ID   DNAK_LYSSH              Reviewed;         611 AA.
AC   O69268;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 98.
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   Lysinibacillus sphaericus (Bacillus sphaericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33203 / 1593;
RA   Ahmad S., Selvapandiyan A., Gasbarri M., Bhatnagar R.K.;
RL   Submitted (SEP-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; Y17157; CAA76663.1; -; Genomic_DNA.
DR   AlphaFoldDB; O69268; -.
DR   SMR; O69268; -.
DR   STRING; 1421.A2J09_11485; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..611
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078418"
FT   REGION          577..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         173
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   611 AA;  65558 MW;  24FA34E461B8AE54 CRC64;
     MSKIIGIDLG TTNSCVSVLE GGEPKVIPNP EGNRTTPSVV AFKNGERQVG EVAKRQSVTN
     PNTIISIKSK MGTAEKVTVE DKDYTPQEVS AMILQYLKGY AEDYLGEKVT KAVITVPAYF
     NDAQRQATKD AGKIAGLEVE RIINEPTAAA LRYGLDKQDQ DQKVLVFDLG GGTFDVSILE
     LGDGVFEVLA TAGDNKLGGD DFDDAIIEYL VAEFKKENGI DLSKDKMAMQ RLKDAAEKAK
     KDLSGVTSTQ ISLPFITAGE AGPLHLEISL TRAKFDEITL PLVNRTVGPV RQALSDAGLS
     TSEIDQVILV GGSTRIPAVQ EAVRKETNKE PHRGVNPDEV VAMGAAVQGG VLTGDVKDVV
     LLDVTPLSLG IETMGGVFTK LIDRNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERSMAAD
     NKTLGRFQLA DIPPAPRGVP QIEVTFDIDK NGIVSVKAKD LGTNKEQTIV IQSDSGLSEA
     EIERMVKDAE ANRDADAKRK EEADLRNEAD QLVFQVDKTI TDLGEQITED EKKSVEDARD
     ELKKALEAGE LEGIKAAKEK LEGVLQPLVM KVYEQAAAAA QARQGGEADA GAGKKDDGVV
     DADFEEVKDD K