ID   DNAK_CLOTE              Reviewed;         618 AA.
AC   Q892R0;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=CTC_02031;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36534.1; -; Genomic_DNA.
DR   RefSeq; WP_011100192.1; NC_004557.1.
DR   AlphaFoldDB; Q892R0; -.
DR   SMR; Q892R0; -.
DR   STRING; 212717.CTC_02031; -.
DR   EnsemblBacteria; AAO36534; AAO36534; CTC_02031.
DR   GeneID; 64179858; -.
DR   KEGG; ctc:CTC_02031; -.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001412; 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   Reference proteome; Stress response.
FT   CHAIN           1..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078451"
FT   REGION          579..618
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   618 AA;  66393 MW;  5699D6EC567C6097 CRC64;
     MAKVIGIDLG TTNSCVSVME GGNPVVITNS EGARTTPSVV SFQDNGERLV GQIAKRQAIT
     NPHKTIMSIK RYMGTDHKET IDGKEYTPQE LSAIILQKLK ADAEAYLGGT VTQAVITVPA
     YFNDSQRQAT KDAGRIAGLE VLRIINEPTA ASLAYGLDKM DTNQKILVYD LGGGTFDVSI
     LELGDGVFEV KSTNGNTKLG GDDFDQRIID HIAETFKKDS GIDLRTDKMA LQRLKEAAEK
     AKIELSSSTQ TNINLPFITA DATGPKHIDM NLTRAKFNEL TQDLVEGTLT PMKKALQDAE
     MSIGEIDKVI LVGGSTRIPA VQDAVKNFTG KEPSKDVNPD ECVAMGAAVQ AGVLTGDVKD
     VLLLDVTPLT LGIETLGGVA TPLIERNTTI PTRKSQVFST AADGQTSVEI HVVQGERQMA
     ADNKTLGRFT LSGIAPAPRG IPQIEVTFDI DANGIVNVSA KDKGTGKEAN ITITASTNLS
     DDEVEKAVND AKKFEEEDKK RKESVEVKNN AEQIFYQTEK TLNELGDKVS AEDKATIEEK
     LNALKGVKDG EDIEAIKKAT EDLTQAFYQI SSKIYQDAGA PGAEGFDSNM AGEANAGQNA
     NNDDNVVDAD YKVEDDEK