ID   DNAK_GEOSM              Reviewed;         640 AA.
AC   C6E643;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=GM21_3574;
OS   Geobacter sp. (strain M21).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) 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; CP001661; ACT19595.1; -; Genomic_DNA.
DR   RefSeq; WP_015838780.1; NC_012918.1.
DR   AlphaFoldDB; C6E643; -.
DR   SMR; C6E643; -.
DR   STRING; 443144.GM21_3574; -.
DR   EnsemblBacteria; ACT19595; ACT19595; GM21_3574.
DR   KEGG; gem:GM21_3574; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_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..640
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205189"
FT   REGION          600..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   640 AA;  68492 MW;  9CD9D134980EA97A CRC64;
     MSRVIGIDLG TTNSCVAVME GGEPVVIANA EGSRTTPSMI AFAESGERLV GQQAKRQAVT
     NPENTLYAIK RLIGRKFDTE AVKKDIAISP FKIVKADNSD AWVEVRGQKY SPPEISAMVL
     QKMKKTAEDY LGETVTDAVI TVPAYFDDSQ RQATKDAGKI AGLNVLRIIN EPTAAALAYG
     LDKKKDEKIA VFDLGGGTFD VSILELGEGV FEVKSTNGDT FLGGEDFDQK IIDHIADEFK
     KDQGIDLRGD KMALQRLKEA GEKAKCELST SLETDINLPF ITADASGPKH LTMKLTRAKL
     ESICAELIAN LEGPCRTALK DAGLSASDID EVILVGGMTR MPIVQKKVQD IFGKVPNRGV
     NPDEVVAIGA AIQGGVLRGD VKDVLLLDVT PLSLGIETLG GVLTKLIDKN STIPCRKSQV
     FSTAADNQPA VSIHVLQGER EMAADNKTLG NFELSGIPSA PRGVPQIEVT FDIDANGIVH
     VSAKDLGTGK EQSIRITASS GLSKEEVEKM VREAEAHAAD DKKKRELIEA KNQADNLIYQ
     TEKSLTEFGD KIDASEKQKI EEGVAALKKA LEGSDADEIK KASDSLMQAS HKLAEAVYAK
     TQGAGAEGSE QPHGEQEAGG AAKGETVVDA DFEEVKDDKK