ID   DNAK_DELAS              Reviewed;         648 AA.
AC   A9BNG5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Daci_5231;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000884; ABX37860.1; -; Genomic_DNA.
DR   RefSeq; WP_012207030.1; NC_010002.1.
DR   AlphaFoldDB; A9BNG5; -.
DR   SMR; A9BNG5; -.
DR   STRING; 398578.Daci_5231; -.
DR   PRIDE; A9BNG5; -.
DR   EnsemblBacteria; ABX37860; ABX37860; Daci_5231.
DR   KEGG; dac:Daci_5231; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000784; 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..648
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119696"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   648 AA;  69129 MW;  3ABB9CC53CA06A7E CRC64;
     MGKIIGIDLG TTNSCVAIMD GNTTRVIENS EGARTTPSII AYQEDGEILV GASAKRQAVT
     NPRNTIYAAK RLIGRKFDEK EVQKDIDLMP YTISRADNGD AWVEVRGQKL APPQISAEVL
     RKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
     LDKTDKGDRK IAVYDLGGGT FDVSIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
     IITEFKKEQG VDLAKDVLAL QRLKEAAEKA KIELSNSAQT DINLPYITAD ASGPKHLNIK
     LTRSKLESLV EDLIERTIAP CRTAIKDAGV SVSDIDDVIL VGGMTRMPKV QEKVKEFFGK
     DPRKDVNPDE AVAVGAAVQG QVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
     TKFAQTFSTA DDNQPAVTIK VFQGEREMAS GNKMLGEFNL EGIPPAARGV PQIEVAFDID
     ANGILNVSAK DKASGKENKI TIKANSGLSE DEIQKMVKDA ELNAADDKKK LELVQARNQG
     EAAVHSVKKS LGEHGDKLDA GEKTAIESAV KDLEEALKGE DKDAIDAKTT ALMTASQKLG
     EKMYADAQAA GGPEAAAAAA AGAAGASAGA AAADDNVVDA EVKEVKKD