ID   DNAK_STRGR              Reviewed;         618 AA.
AC   Q54215;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-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   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HUT 6037 NO.2247;
RA   Hatada Y.;
RT   "Cloning and nucleotide sequence of a hsp70 gene from Streptomyces
RT   griseus.";
RL   J. Ferment. Bioeng. 77:461-477(1994).
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; D14499; BAA03389.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54215; -.
DR   SMR; Q54215; -.
DR   STRING; 1911.GCA_001715295_03077; -.
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   CHAIN           1..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078551"
FT   REGION          489..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..618
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   618 AA;  66619 MW;  0E5275D9C5BBF465 CRC64;
     MARAVGIDLG TTNSVVSVLE GGEPTVITNA EGARTTPSVV AFAKNGEVLV GEVAKRQAVT
     NVDRTIRSVK RHMGTDWKID LDGKSFNPQQ MSAFILQKLK RDAESYLGEK VTDAVITVPA
     YFNDSERQAT KEAGEIAGLN VLRIVNEPTA AALAYGLDKD DQTILVFDLG GGTFDVSLLE
     IGDGVVEVKA TNGDNHLGGD DWDQRVVDYL VKQFANGHGV DLSKDKMALQ RLREAAEKAK
     IELSSSTETT INLPYITASA EGPLHLDEKL TRSQFQQLTA DLLDRCKTPF HNVIKDAGIQ
     LSEIDHVVLV GGSTRMPAVA ELVKELTGGQ EANKGVNPDE VVAIGASLQA GVLKGEVKDV
     LLLDVTPLSL GIETKGGIMT KLIERNTTIP TKRSEIFTTA EDNQPSVQIQ VYQGEREIAA
     YNKKLGMFEL TGLPPAPRGV PQIEVAFDID ANGIMHVAAK DLGTGKEQKM TVTGGSSLPK
     DEVNRMREEA EKYAEEDHAR REAAESRNQG EQLVYQTEKF LKDNEDKVPA DVKTEVETAV
     GELKEKLKGE DSAEIRTATE KVRGRLPRIW ARRCTANAQA EGAAPGADAP GDAQAKADDD
     VVDAEIVDDE KDTKGGAA