ID   DNAK_GLUOX              Reviewed;         634 AA.
AC   Q5FSL5; Q3LG59;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=GOX0857;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRIC 1504;
RA   Okamoto-Kainuma A., Chen Y., Harada K., Ishikawa M., Fukaya M.,
RA   Tsukamoto Y., Koizumi Y.;
RT   "Characterization of the groESL and the dnaKJ genes of Gluconobacter
RT   oxydans NRIC 1504.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; AB211147; BAE46550.1; -; Genomic_RNA.
DR   EMBL; CP000009; AAW60631.1; -; Genomic_DNA.
DR   RefSeq; WP_011252427.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FSL5; -.
DR   SMR; Q5FSL5; -.
DR   STRING; 290633.GOX0857; -.
DR   EnsemblBacteria; AAW60631; AAW60631; GOX0857.
DR   KEGG; gox:GOX0857; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000006375; 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; 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..634
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225968"
FT   REGION          601..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..634
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"
FT   CONFLICT        463
FT                   /note="G -> A (in Ref. 1; BAE46550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        529..530
FT                   /note="EL -> DV (in Ref. 1; BAE46550)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   634 AA;  67711 MW;  E6D3BF5F94488938 CRC64;
     MSKVIGIDLG TTNSCVAVRE GDETKVIENS EGARTTPSMV AFTDNGERLV GQAAKRQAVT
     NPANTLYAVK RLIGRRYDDP TVQKDKEMVP YAIVRGDNGD AWVEARGEKY APSQIAAYVL
     GKMKETAESY LGETVSQAVI TVPAYFNDAQ RQATRDAGKI AGLEVLRIIN EPTAAALAYG
     LGKRDSGTVA VYDLGGGTFD VSILEISDGV IEVKSTNGDT FLGGEDFDNR IIGFLADEFK
     KDQGIDLRGD KLALQRLKEA AEKAKIELSS SKETEINLPF ITADASGPKH LVVKLSRAKL
     ESLVDDLIQR TLGPCRAAIK DASVSANEID EVILVGGMTR MPKVIETVKE FFGKDPARNV
     NPDEVVAIGA AVQGAVLKGD VKDVLLLDVT PLSLGIETLG GVFTRLIDRN TTIPTKKSQT
     FSTAEDNQNA VTIKVYQGER EMAADNKLLG NFDLQGIAPA PRGVPQIEVT FDIDANGIVN
     VSAKDKATNK EQQIKIQASG GLSDADIDRM VKDAEANASA DKAKRELVEL RNSTESLIHQ
     TEKSITEGGD KVPAADKSEA EAAIAEAREA LGGENLDTLK AASEKLTQAA MKVGQGVYQA
     GQGAEGGAAP EGEKKDENVV DADFEDLEDD SKKH