ID   DNAK_STRGG              Reviewed;         617 AA.
AC   B1VMF3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=SGR_3434;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; AP009493; BAG20263.1; -; Genomic_DNA.
DR   RefSeq; WP_003967578.1; NC_010572.1.
DR   AlphaFoldDB; B1VMF3; -.
DR   SMR; B1VMF3; -.
DR   STRING; 455632.SGR_3434; -.
DR   PRIDE; B1VMF3; -.
DR   EnsemblBacteria; BAG20263; BAG20263; SGR_3434.
DR   GeneID; 6212360; -.
DR   KEGG; sgr:SGR_3434; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001685; Chromosome.
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..617
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119759"
FT   REGION          489..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..617
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        592..617
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:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   617 AA;  66244 MW;  7B0009AC11B36DB6 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 KVAAVSQKLG QAMYANAQAE GAAPGADAPG DAQAKADDDV
     VDAEIVDDEK DTKGGAA