ID   DNAK_COXB2              Reviewed;         656 AA.
AC   B6IZJ0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=CbuG_0718;
OS   Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CbuG_Q212;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
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; CP001019; ACJ18118.1; -; Genomic_DNA.
DR   RefSeq; WP_012569898.1; NC_011527.1.
DR   AlphaFoldDB; B6IZJ0; -.
DR   SMR; B6IZJ0; -.
DR   KEGG; cbg:CbuG_0718; -.
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_1000119694"
FT   REGION          602..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;  70838 MW;  CC333A63DDCE3B52 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 EKVVNELKEA MKGNDKDAIE AKRKALTEHS
     SKLAERVYAK KGGAAGAPPG GEAEGEPQAQ AGGKKEDVVD AEFEEVKDEK KKDEDK