DNAK_ACIET
ID DNAK_ACIET Reviewed; 646 AA.
AC B9MDJ7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=Dtpsy_2571;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Diaphorobacter.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) 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; CP001392; ACM34006.1; -; Genomic_DNA.
DR RefSeq; WP_015913929.1; NC_011992.1.
DR AlphaFoldDB; B9MDJ7; -.
DR SMR; B9MDJ7; -.
DR STRING; 535289.Dtpsy_2571; -.
DR EnsemblBacteria; ACM34006; ACM34006; Dtpsy_2571.
DR KEGG; dia:Dtpsy_2571; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000450; 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 Stress response.
FT CHAIN 1..646
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133144"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 646 AA; 69181 MW; F2C226A62B1D0AC1 CRC64;
MGKIIGIDLG TTNSCVAIME GNNTRVIENS EGARTTPSII AYQEDGEILV GASAKRQAVT
NPKNTIYAAK RLIGRKFEEK EVQKDIDLMP FTITRADNGD AWVEVRGQKL APPQISAEVL
RKMKKTAEDF LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
LDKQDKGDRK IAVYDLGGGT FDVSIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
IIGEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSNSAQT DINLPYITAD ASGPKHLNIK
LTRAKLESLV DELIERTIAP CRTAIKDAGI SVSDINDVIL VGGMTRMPKV QEKVKEFFGK
EPRKDVNPDE AVAVGAAIQG QVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
TKFAQTFSTA EDNQPAVTIK VFQGEREIAS ANKLLGEFNL EGIPPASRGT PQIEVTFDID
ANGILHVGAK DKGTGKENKI TIKANSGLSE DEIQKMVKDA ELNAADDKKK LELVQARNQG
EAAVHTVNKS LSEHGDKLDA GEKEKIEAAV KDLEAALKTE DKAAIDEKTT ALMAASQKLG
EKMYGDAQAA QGAEAAAAQA AAGGSAGAAA QDDNVVDAEV KEVKKG
