ID   DNAK_COXBR              Reviewed;         656 AA.
AC   A9N8H2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, 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};
GN   OrderedLocusNames=COXBURSA331_A1439;
OS   Coxiella burnetii (strain RSA 331 / Henzerling II).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=360115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 331 / Henzerling II;
RA   Seshadri R., Samuel J.E.;
RT   "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT   burnetii isolates.";
RL   Submitted (NOV-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; CP000890; ABX78431.1; -; Genomic_DNA.
DR   RefSeq; WP_005770882.1; NC_010117.1.
DR   AlphaFoldDB; A9N8H2; -.
DR   SMR; A9N8H2; -.
DR   KEGG; cbs:COXBURSA331_A1439; -.
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..656
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000079223"
FT   REGION          607..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         204
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   656 AA;  70755 MW;  4FF43FDED22973FB CRC64;
     MAEIIGIDLG TTNSCVAVME GGKVRVIENA EGSRTTPSIV AYTKDGEVLV GASAKRQAVT
     NADRTLYAIK RLIGRRFDDN VVQKDIKMVP YKIIKADNGD AWVEVKDKEG KSQKLAPPQI
     SAQVLIKMKK TAEDYLGHEV KDAVITVPAY FNDSQRQATK DAGKIAGLNV KRIINEPTAA
     ALAYGMDKKK GDRKIAVYDL GGGTFDISII EIAEVDGEHQ FEVLATNGDT FLGGEDFDLR
     LIDYLAGEFK KDEGVDLHND PLALQRLKEA AEKAKIELSS SQQTDVNLPY ITADASGPKH
     LNIRLTRAKL ESLVEDLVER TIEPCKVAIK DAGLKVSEID DVILVGGQTR MPKVQEAVKN
     FFGKEARKDV NPDEAVAIGA AIQGAVLSGE VKDVLLLDVT PLSLGIETLG GVMTKLIEKN
     TTIPTKANQV FSTADDNQTA VTVHVLQGER EMASANKSLG RFDLSDIPPA PRGVPQIEVT
     FDIDANGILH VSAKDKATGK EQSIVIKASS GLSDEEVEKM VKDAEAHRDS DRKFHELVDA
     RNQADAMIHA AEKSVKDLGS EVSADEKSAI EKAVNELKEA MKGNDKDAIE AKTKALTEHS
     SKLAERVYAK KGGAAGAPPG GEAEGEPQAQ AGGKKEDVVD AEFEEVKDEK KKDEDK