ID   DNAK_POLNS              Reviewed;         640 AA.
AC   B1XRU1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Pnec_1484;
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1;
RX   PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA   Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA   Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT   "Polynucleobacter necessarius, a model for genome reduction in both free-
RT   living and symbiotic bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB44576.1; -; Genomic_DNA.
DR   RefSeq; WP_012358336.1; NC_010531.1.
DR   AlphaFoldDB; B1XRU1; -.
DR   SMR; B1XRU1; -.
DR   STRING; 452638.Pnec_1484; -.
DR   EnsemblBacteria; ACB44576; ACB44576; Pnec_1484.
DR   KEGG; pne:Pnec_1484; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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_1000119738"
FT   REGION          608..628
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   640 AA;  68480 MW;  AD7D984808FAE36C CRC64;
     MGKIIGIDLG TTNSCVSVVE NNAPKVVENA EGARTTPSII AYVEDGEVLV GAPAKRQSVT
     NPKNTIYAVK RLMGRKFTDP EVQKDIGLMP YAIIQADNGD AWVEARDKKM APQQVSAEIL
     RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
     LDKQDKVDRK IAVYDLGGGT FDVSIIEIAN VDGEKQFEVL STNGDTFLGG EDFDQRIIDW
     IIAEFKKEQG VDLSKDVLAL QRLKDAAEKA KIELSSAQQT EINLPYVTAD AGGPKHLNLK
     LTRAKLESLV EELINRTAGP CLTAIKDAGV SVANIDDVIL VGGQTRMPAV QDKVKEIFGK
     EPRKDVNPDE AVAVGAAIQG SVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMIPKNTTIP
     TKHSQVYSTA EDNQPAVTIK CFQGEREMAA ANKLLGEFNL EGIAPAQRGM PQIEVTFDID
     ANGILHVTAK DKNTGKENKI TIKANSGLTE EEIQRMVKDA EANAAEDKKA LELVTARNTA
     DALAHSTKKA LEEHGASLEA TEKEAIEAAL KDLDEAIKGS DKEAIDTKTE ALGKASQKLG
     EKVMAAEQAK AGAAPGGAAP GTASDADVVD ADFKEVDDKK