ID   DNAK_POLNA              Reviewed;         647 AA.
AC   A1VMG2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Pnap_1526;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(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; CP000529; ABM36840.1; -; Genomic_DNA.
DR   RefSeq; WP_011800927.1; NC_008781.1.
DR   AlphaFoldDB; A1VMG2; -.
DR   SMR; A1VMG2; -.
DR   STRING; 365044.Pnap_1526; -.
DR   EnsemblBacteria; ABM36840; ABM36840; Pnap_1526.
DR   KEGG; pna:Pnap_1526; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000644; 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_1000059627"
FT   REGION          606..647
FT                   /note="Disordered"
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;  69418 MW;  CE80504D365F09C4 CRC64;
     MGRIIGIDLG TTNSCVSIME GNTPRVIENS EGARTTPSIV AYQEDGEVLV GASAKRQAVT
     NPKNTLYAVK RLIGRKFTEK EVQKDIGLMP YSIVPADNGD AWIEVRGKKL SAQQVSADIL
     RKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
     LDKQEKGDRK IAVYDLGGGT FDISIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDF
     IIDEFKKDSG VNLKNDVLAL QRLKEAAEKA KIELSNSAQT DINLPYITAD ASGPKHLNIK
     MTRAKLESLV EELIERTIAP CRVAVKDAGV SVGDIHDVIL VGGMTRMPKV QEKVKEFFGK
     EPRKDVNPDE AVAVGAAIQG QVLSGDRSDV LLLDVTPLSL GIETMGGVMT KMIKKNTTIP
     TKFAQTFSTA EDNQPAVTIK VFQGEREIAS GNKALGEFNL EGIPPASRGT PQIEVSFDID
     ANGILHVGAK DKGTGKENKI TIKANSGLTE AEIQQMVKDA ELNAEDDKKK VEFVQAKNSA
     EAMVHSVKKS LGEYGDKLDA GEKAKIEAAI KDMEEALKSD DKAAIEAKNA ALMEASQKLG
     EKMYADMQSS QAAGGDAGAA AGAEHAQAKP AADDNVVDAE VKEVKKG