ID   DNAK_CLOK5              Reviewed;         618 AA.
AC   A5N6M2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=CKL_0902;
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(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; CP000673; EDK32953.1; -; Genomic_DNA.
DR   RefSeq; WP_012101282.1; NC_009706.1.
DR   AlphaFoldDB; A5N6M2; -.
DR   SMR; A5N6M2; -.
DR   STRING; 431943.CKL_0902; -.
DR   EnsemblBacteria; EDK32953; EDK32953; CKL_0902.
DR   KEGG; ckl:CKL_0902; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_3_0_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002411; 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_1000079220"
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