ID   DNAK_LEGPA              Reviewed;         644 AA.
AC   Q5X3M7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=lpp2007;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628336; CAH13159.1; -; Genomic_DNA.
DR   RefSeq; WP_011214271.1; NC_006368.1.
DR   AlphaFoldDB; Q5X3M7; -.
DR   SMR; Q5X3M7; -.
DR   KEGG; lpp:lpp2007; -.
DR   LegioList; lpp2007; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
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..644
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225974"
FT   REGION          605..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..644
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   644 AA;  70118 MW;  8B30A50FBB1BF5B2 CRC64;
     MAKIIGIDLG TTNSCVAVME GDKPKVIENS EGHRTTPSIV AFTDDNEILV GQSAKRQSVT
     NPEKTLFAIK RLIGRRFDDP IVQKDIKMVP YKIMKADNGD AWVRVKDQDK APPQISAEVL
     RKMKKTAEDY LGEEVKEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
     MDKKRGDSVI AVYDLGGGTF DISIIEIAEV DGEHQFEVLA TNGDTFLGGE DFDLALIEYL
     ASEFKKDTGI DLHNDPLALQ RLKEAAEKAK IELSSAQQTD VNLPYITADA SGPKHLNIKL
     TRAKLESLVE KLVERTIEPC KTALKDAGLT VSQINEVILV GGQTRMPLVQ KTVEEFFGKE
     PRKDVNPDEA VAVGAAIQAA VLSGEVKDIL LLDVTPLSLG IETMGGVMTK LIEKNTTIPT
     KATQVFSTAD DNQTAVTVHV LQGEREQASA NKSLGRFDLR DIPPAPRGVP QIEVTFDIDA
     NGILNVSAKD KATGKAQSIV IKASSGLSEE EVAAMVKDAQ SHAEEDKKFK EMAELRNQAD
     SLIHSCEKSM KDLADELSED EKKGIETAIS ELKEAVQGTD KTRIEDKLKV LTDASAKMAE
     RIYAKKSSEG QAAQGQTQSQ ESTKPVEEGV VDAEFEEVKE EDKK