ID   DNAK_CAMJD              Reviewed;         623 AA.
AC   A7H484;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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};
GN   OrderedLocusNames=JJD26997_1258;
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) 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; CP000768; ABS44458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H484; -.
DR   SMR; A7H484; -.
DR   PRIDE; A7H484; -.
DR   EnsemblBacteria; ABS44458; ABS44458; JJD26997_1258.
DR   KEGG; cjd:JJD26997_1258; -.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002302; 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; 1.
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..623
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059532"
FT   REGION          595..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   623 AA;  67478 MW;  F94CC92E2D3B79CA CRC64;
     MSKVIGIDLG TTNSCVAVYE RGESKVIPNK EGKNTTPSVV AFTDKGEVLV GDSAKRQAVT
     NPEKTIYSIK RIMGLMINED AAKEAKTRLP YHITERNGAC AIEIAGKIYT PQEISAKVLM
     KLKEDAEAFL GESVVDAVIT VPAYFNDAQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
     DKKDSEKIVV YDLGGGTFDV TVLETGDNVV EVLATGGNAF LGGDDFDNKL IDFLANEFKD
     ETGIDLKNDV MALQRLKEAA ENAKKELSSA NETEINLPFI TADASGPKHL VKKLTRAKFE
     GMIDSLVAET ITKINEVVSD AGLKKDEIKE VVMVGGSTRV PLVQEEVKKT FNKDLNKSVN
     PDEVVAIGAA IQGAVIKGDV KDVLLLDVTP LSLGIETLGG VMTKIIEKGT TIPTKKEQVF
     STAEDNQSAV TINVLQGERE FSRDNKSLGN FNLEGIPPAP RGMPQIEVTF DIDANGILTV
     SAKDKATGKA QEIKITGSSG LSEEEINNMV KDAELHKEED KKRKEAVDVR NAADSLAHQV
     EKSLSELGEK VATADKENIQ KALDDLRETL KNQNASKEEI ESKMKALSEV SHKLAENMYK
     KDEPNTANDK KKKDDDVIDA EVE