ID   DNAK_CAMJ8              Reviewed;         623 AA.
AC   A8FLH2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=C8J_0710;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
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; CP000814; ABV52309.1; -; Genomic_DNA.
DR   RefSeq; WP_002856760.1; NC_009839.1.
DR   AlphaFoldDB; A8FLH2; -.
DR   SMR; A8FLH2; -.
DR   KEGG; cju:C8J_0710; -.
DR   HOGENOM; CLU_005965_2_4_7; -.
DR   OMA; ISIKRHM; -.
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_1000072034"
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;  67416 MW;  034B64FE0D977505 CRC64;
     MSKVIGIDLG TTNSCVAVYE RGESKVIPNK EGKNTTPSVV AFTDKGEVLV GDSAKRQAVT
     NPEKTIYSIK RIMGLMINED AAKEAKNRLP YHITERNGAC AIEIAGKIYT PQEISAKVLM
     KLKEDAEAFL GESVVDAVIT VPAYFNDAQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
     DKKDSEKIVV YDLGGGTFDV TVLETGDNVV EVLATGGNAF LGGDDFDNKL IDFLANEFKD
     ETGIDLKNDV MALQRLKEAA ENAKKELSSA NETEINLPFI TADASGPKHL VKKLTRAKFE
     GMIDSLVAET ITKINEVVSD AGLKKDEIKE IVMVGGSTRV PLVQEEVKKA FNKDLNKSVN
     PDEVVAIGAA IQGAVIKGDV KDVLLLDVTP LSLGIETLGG VMTKIIEKGT TIPTKKEQVF
     STAEDNQSAV TINVLQGERE FSRDNKSLGN FNLEGIPPAP RGMPQIEVTF DIDANGILTV
     SAKDKATGKA QEIKITGSSG LSEEEINNMV KDAELHKEED KKRKEAVDAR NAADSLAHQV
     EKSLSELGEK VAAADKENIQ KALDDLRETL KNQNASKEEI ESKMKALSEV SHKLAENMYK
     KDEPNTANDK KKKDDDVIDA EVE