ID   DNAK_DEHMC              Reviewed;         636 AA.
AC   Q3ZYV1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=cbdbA1358;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(2005).
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; AJ965256; CAI83407.1; -; Genomic_DNA.
DR   RefSeq; WP_011309758.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZYV1; -.
DR   SMR; Q3ZYV1; -.
DR   KEGG; deh:cbdbA1358; -.
DR   HOGENOM; CLU_005965_0_0_0; -.
DR   OMA; DKMVLQR; -.
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; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 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..636
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225957"
FT   REGION          602..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         203
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   636 AA;  68519 MW;  9555F5BA7E5CAD9B CRC64;
     MGKVVGIDLG TTNSEVAVMQ GGEPVVIPSA EGSTLIPSVV AINKNGERIV GRQAKNQAIL
     NPENTVYSIK RFMGRKWGEP AGRELPVEAD AKRKPYKVIQ GNNNEVRVVM GDKDFSPPEV
     SAMILQKLKS DAEAYLGEKV TEAVITVPAY FNDAQRQATK DAGAIAGLKV LRIINEPTAA
     ALAYGLDKKK DETIAVYDLG GGTFDISILE LGEGTFQVKS TAGDTHLGGD DFDQKIIDWL
     IAEYKKDQGI DLSKDKTALQ RLKEAAEKAK IELSTVQQTE INLPFITADA SGPKHLNIIL
     TRSKLEQMVM DLVEKSLEPC RQALKDSGKT SAEINEVILV GGQTRMPLVQ QKVKDFFGKE
     PNKGVNPDEV VAIGAAIQAG VLKGEVSDVL LLDVIPLTLG IETLGGVSTA LITRNTTIPT
     SKSQVFSTAA DNQPSVEIHV LQGERPMAAD NRTLGRFMLD GILPAPRGVP QIEVTFDIDA
     NGMLSVKAKD KGTGREQKIT ITASSGLSKE EVEKMTREAE AHAVEDTKRK EEIEARNVAD
     NLAYNAEKTL RDNKDKIPAE LNTELESKIA AVRTALQGND VEAIKKTTQE LSTALQSVGS
     AVYGKQQEGA PAQEEPSAEG KKADDEGTVE GEFREV