ID   DNAK_POLSJ              Reviewed;         647 AA.
AC   Q128K2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Bpro_3126;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE45040.1; -; Genomic_DNA.
DR   RefSeq; WP_011484035.1; NC_007948.1.
DR   AlphaFoldDB; Q128K2; -.
DR   SMR; Q128K2; -.
DR   STRING; 296591.Bpro_3126; -.
DR   EnsemblBacteria; ABE45040; ABE45040; Bpro_3126.
DR   KEGG; pol:Bpro_3126; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001983; 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..647
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059628"
FT   REGION          607..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   647 AA;  69535 MW;  DB0E6F0E56962AC7 CRC64;
     MGRIIGIDLG TTNSCVSIME GNTPRVIENS EGARTTPSIV AYQEDGEVLV GASAKRQAVT
     NAKNTLYAIK RLIGRKFTEK EVQKDINLMP YKIAAADNGD AWVEVRGKQI SAQQVSADIL
     RKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
     LDKQEKGDRK IAVYDLGGGT FDISIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
     IIAEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSNSAQT DINLPYITAD ASGPKHLNIK
     LSRAKLEALV EELLERTLAP CRTAIKDAGV SVGDIHDVIL VGGQTRMPKV QEMVKALFGK
     EPRKDVNPDE AVAVGAAIQG QVLSGDRTDV LLLDVTPLSL GIETMGGVMT KMIKKNTTIP
     TKFAQTFSTA EDNQPAVTIK VFQGEREIAS GNKALGEFNL EGIPPAARGT PQIEVSFDID
     ANGILHVGAK DKGTGKENKI TIKANSGLSE AEIQQMVKDA ELHSADDKKK VEFVQAKNNA
     EAMVHSVRKS LGEYGDKLEV GEKEKIETAI KDMEEALKGD DKDAIEAKNT ALMEASQKLG
     EKMYADMQSS QAAGAEAAAG GAGAEQAHAK PADDNVVDAE VKEVKKG