ID   DNAK_GRABC              Reviewed;         632 AA.
AC   Q0BW82;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=GbCGDNIH1_0022;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI60920.1; -; Genomic_DNA.
DR   RefSeq; WP_011630730.1; NC_008343.2.
DR   AlphaFoldDB; Q0BW82; -.
DR   SMR; Q0BW82; -.
DR   STRING; 391165.GbCGDNIH1_0022; -.
DR   PRIDE; Q0BW82; -.
DR   EnsemblBacteria; ABI60920; ABI60920; GbCGDNIH1_0022.
DR   KEGG; gbe:GbCGDNIH1_0022; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_5; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001963; 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   Reference proteome; Stress response.
FT   CHAIN           1..632
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059569"
FT   REGION          600..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..632
FT                   /note="Basic and acidic residues"
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   632 AA;  67860 MW;  D6AF0477DD7F2073 CRC64;
     MSKVIGIDLG TTNSCVAIME GKDVRVLENA EGARTTPSMI AFTDSGERLV GQAAKRQAVT
     NPSNTLYAVK RLIGRRYDDP TVAKDKDLVP YAIVRGDNGD AWVEARGEKY APSQISAFVL
     SKMKETAEAY LGEPVTQAVI TVPAYFNDSQ RQATKDAGRI AGLEVLRIIN EPTAAALAYG
     MDKKNTGTIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDAR VIDYLASEFQ
     REQGIDLRKD KLALQRLKEA AEKAKIELSS SKETEINLPF ITADASGPKH LVLKLSRAKL
     ESLVDDLIQR TLEPCRKALK DAGVSAGEIS DVILVGGMTR MPKVIEAVKQ FFGKEPARNV
     NPDEVVAIGA AVQGAVLKGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQV
     FSTAEDNQPA VTIKVYQGER EMAADNKSLG QFDLTGLPPA PRGVPQIEVT FDIDANGIVN
     VSAKDKATGK EQQIRIQASG GLSDADIQRM VQEAEANAEA DKQRRALVEA RNQAESLVHQ
     VEKNLKEQGD KIAEADKGEA ESAISATRTA LEGDDLAALT QATERLSQVA MKIGEAMYKA
     QSEAPTGEAE AGPNGEKVVD ADFEEVDPKK HS