ID   DNAK_CLOPS              Reviewed;         619 AA.
AC   Q0SRE3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=CPR_2005;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000312; ABG86480.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SRE3; -.
DR   SMR; Q0SRE3; -.
DR   EnsemblBacteria; ABG86480; ABG86480; CPR_2005.
DR   KEGG; cpr:CPR_2005; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001824; 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   Stress response.
FT   CHAIN           1..619
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059545"
FT   REGION          578..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   619 AA;  66497 MW;  E659CCA96A0513E3 CRC64;
     MSKIIGIDLG TTNSCVAVME GGEPVVITNS EGARTTPSVV SFQANGERLV GQVAKRQAIT
     NPEKTIMSIK RHMGTDYKVN IDGKDYTPQE ISAMILQKLK ADAEAYLGEK VTEAVITVPA
     YFNDAERQAT KDAGRIAGLD VKRIINEPTA ASLAYGLDKM DSAHKILVYD LGGGTFDVSI
     LDLGDGVFEV VSTNGDARLG GDDFDQRIID YIAEDFKAQN GIDLRQDKMA LQRLKEAAEK
     AKIELSSSTQ TLINLPFITA DATGPKHIDM TLTRAKFNEL THDLVERTID IMKEALKSGN
     VSLNDIDKVI LVGGSTRIPA VQEAVKNFTG KEPSKGVNPD ECVAMGAAIQ AGVLTGDVKD
     VLLLDVTPLT LGIETLGGVA TPLIERNTTI PARKSQIFST AADNQTSVEI HVVQGERQMA
     ADNKTLGRFT LSGIAPAPRG IPQIEVAFDI DANGIVKVSA TDKATGKEAN ITITASTNLS
     DAEIDKAVKE AEQFAEEDKK RKEAIEVKNN AEQIVYQTEK TLNELGDKVS AEEKSEIEAK
     IEEVKKVKDG DDIEAIKKAM EDLTQAFYKI SEKLYQQNGG AQGEGFDPNN MGGANAGTGA
     ANSNDDNVVD ADFEVQDDK