ID   DNAK_HELP2              Reviewed;         620 AA.
AC   B6JPL0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=HPP12_0111;
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12;
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-2008) 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; CP001217; ACJ07271.1; -; Genomic_DNA.
DR   RefSeq; WP_000521012.1; NC_011498.1.
DR   AlphaFoldDB; B6JPL0; -.
DR   SMR; B6JPL0; -.
DR   EnsemblBacteria; ACJ07271; ACJ07271; HPP12_0111.
DR   KEGG; hpp:HPP12_0111; -.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008198; 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..620
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119712"
FT   REGION          597..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..620
FT                   /note="Basic and acidic residues"
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   620 AA;  67095 MW;  8C90E2EE4487C03F CRC64;
     MGKVIGIDLG TTNSAMAVYE GNEAKIIANK EGKNTTPSIV AFTDKGEILV GESAKRQAVT
     NPEKTIYSIK RIMGLMFNED KAKEAEKRLP YKIVDRNGAC AIEISGKVYT PQEISAKILM
     KLKEDAESYL GESVTEAVIT VPAYFNDSQR KATKEAGTIA GLNVLRIINE PTSAALAYGL
     DKKESEKIMV YDLGGGTFDV TVLETGDNVV EVLATGGDAF LGGDDFDNRV IDFLASEFKS
     ETGIEIKNDV MALQRLKEAA ENAKKELSSA METEINLPFI TADATGPKHL VKKLTRAKFE
     SLTEDLMEET ISKIESVIKD AGLTKNEISE VVMVGGSTRI PKVQERVKAF INKELNKSVN
     PDEVVAVGAS IQGGVLKGDV KDVLLLDVTP LSLGIETLGG VMTKVIDRGT TIPAKKSQVF
     STAEDNQPAV SIMVLQGERE LARDNKSLGK FDLQGIAPAP RGVPQIEVTF DIDANGILTV
     SAQDKNTGKS QEIKISGSSG LSDSEIEKMV KDAELHKEED ARKKEVIEAR NHADSLAHQT
     QKSLDEHKTN LNENDANEIQ NAINALKDCV KNDNATKAEL EDKTKLLAQA AQKLGEAMAN
     KNNAEQPKKK DDDVIDAEVE