ID   DNAK_CLOK1              Reviewed;         618 AA.
AC   B9E041;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=CKR_0815;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; AP009049; BAH05866.1; -; Genomic_DNA.
DR   RefSeq; WP_012101282.1; NC_011837.1.
DR   AlphaFoldDB; B9E041; -.
DR   SMR; B9E041; -.
DR   EnsemblBacteria; BAH05866; BAH05866; CKR_0815.
DR   KEGG; ckr:CKR_0815; -.
DR   HOGENOM; CLU_005965_3_0_9; -.
DR   Proteomes; UP000007969; 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..618
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000133140"
FT   REGION          576..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..618
FT                   /note="Basic and acidic residues"
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;  66050 MW;  E262496D15A01A1E CRC64;
     MSKVIGIDLG TTNSCVAVME GGDPVVIANS EGARTTPSVV SFQANGERLV GQVAKRQSIT
     NPDKTIISIK REMGTNHKVN IDGKQYTPQE ISAMVLQKIK ADAEAYLGET VTQAVITVPA
     YFNDSQRQAT KDAGKIAGLE VLRIINEPTA AALAYGMDKM DTNQKIFVYD LGGGTFDVSI
     LELGDGVFEV KATNGDTHLG GDDFDKKIID YIADTFKADN GIDLKNDKMA LQRLKEAAEK
     AKIELSSSTQ TNINLPFITA DATGPKHIDM SLTRAKFNEL TQDLVDRTIE PMKKALNDAG
     LTINDINKVI LVGGSTRIPA VQEAVKSFTG KEPSKGVNPD ECVAMGAAIQ AGVLTGDVKD
     VLLLDVTPLT LGIETLGGVA TPLIERNTTI PTKKSQVFST AADGQTSVEI HVVQGERQMA
     ADNKTLGRFT LSGIAPAPRG VPQIEVTFDI DANGIVNVSA KDKGTGKEAN ITITASTNLS
     DDEIDKAVKE AEKFEEQDKK RKESIEIKNN ADQVVYQTEK TLKDLGDKVS SEDKKAIEEK
     VEAVKKVKDG DDLEAIKKAT EDLTQTFYGI SSKIYSQNAE PGADGGANSG ANPGGTTGNT
     DTKDDNVVDA EYKVDDDK