ID   DNAK_STRCO              Reviewed;         618 AA.
AC   Q05558; Q9KYQ2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 141.
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; OrderedLocusNames=SCO3671; ORFNames=SCH44.11c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=8344522; DOI=10.1016/0378-1119(93)90358-a;
RA   Bucca G., Smith C.P., Alberti M., Seidita G., Passantino R., Puglia A.M.;
RT   "Cloning and sequencing of the dnaK region of Streptomyces coelicolor
RT   A3(2).";
RL   Gene 130:141-144(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=8722574; DOI=10.3109/10425179609010207;
RA   Brans A., Loriaux A., Joris B., Dusart J.;
RT   "Cloning and sequencing of the dnaK locus in Streptomyces coelicolor
RT   A3(2).";
RL   DNA Seq. 6:179-184(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; L46700; AAB29451.1; -; Genomic_DNA.
DR   EMBL; X77458; CAA54606.1; -; Genomic_DNA.
DR   EMBL; AL939117; CAD55329.1; -; Genomic_DNA.
DR   PIR; JN0830; JN0830.
DR   RefSeq; NP_733614.1; NC_003888.3.
DR   RefSeq; WP_003975268.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q05558; -.
DR   SMR; Q05558; -.
DR   STRING; 100226.SCO3671; -.
DR   PRIDE; Q05558; -.
DR   GeneID; 1099107; -.
DR   KEGG; sco:SCO3671; -.
DR   PATRIC; fig|100226.15.peg.3729; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   InParanoid; Q05558; -.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; Q05558; -.
DR   Proteomes; UP000001973; 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; 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   Reference proteome; Stress response.
FT   CHAIN           1..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078550"
FT   REGION          487..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..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;  66270 MW;  3735D39BD14A0511 CRC64;
     MARAVGIDLG TTNSVVSVLE GGEPTVITNA EGARTTPSVV AFAKNGEVLV GEVAKRQAVT
     NVDRTIRSVK RHMGTDWKVN LDGKDFNPQQ ISAFVLQKLK RDAESYLGEK VTDAVITVPA
     YFNDAERQAT KEAGEIAGLN VLRIVNEPTA AALAYGLDKD EQVILVFDLG GGTFDVSLLE
     IGDGVVEVKA TNGDNNLGGD DWDQRVVDYL VKQFQSGHGV DLAKDKMALQ RLREAAEKAK
     IELSSSTETT INLPYITASA EGPLHLDEKL TRAQFQQLTS DLLERCKTPF HNVIKDAGIQ
     LSEIDHVVLV GGSTRMPAVA ELVKELTGGK DANKGVNPDE VVAIGAALQA GVLKGEVKDV
     LLLDVTPLSL GIETKGGIMT KLIERNTTIP TKRSEIFTTA EDNQPSVQIQ VYQGEREIAA
     YNKKLGMFEL TGLPPAPRGV PQIEVAFDID ANGIMHVTAK DLGTGKEQKM TVTGGSSLPK
     DEVDRMRQEA EKYAEEDHAR REAAESRNQG EQLVYQTEKF LKDNEDKVPG EVKTEVESAV
     AELKEKLKGE DTAEIRTATE KVAAVSQKLG QAMYADAQAA QAAGGEAPGA DAGAEGKGAD
     DDVVDAEIVD DERKDGAA