DNAK_ACISJ
ID DNAK_ACISJ Reviewed; 646 AA.
AC A1WAR6;
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=Ajs_3218;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL Submitted (DEC-2006) 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; CP000539; ABM43341.1; -; Genomic_DNA.
DR RefSeq; WP_011806339.1; NC_008782.1.
DR AlphaFoldDB; A1WAR6; -.
DR SMR; A1WAR6; -.
DR STRING; 232721.Ajs_3218; -.
DR EnsemblBacteria; ABM43341; ABM43341; Ajs_3218.
DR KEGG; ajs:Ajs_3218; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000645; 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..646
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059499"
FT REGION 606..646
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 646 AA; 69187 MW; 52B3D43BE2844857 CRC64;
MGKIIGIDLG TTNSCVAIME GNNTRVIENS EGARTTPSII AYQEDGEILV GASAKRQAVT
NPKNTIYAAK RLIGRKFDEK EVQKDIDLMP FTITRADNGD AWVEVRGQKL APPQISAEVL
RKMKKTAEDF LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
LDKQDKGDRK IAVYDLGGGT FDVSIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
IIGEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSNSSQT DINLPYITAD ASGPKHLNIK
LTRAKLESLV EDLIERTIAP CRTAIKDAGI SVSDIDDVIL VGGMTRMPKV QEKVKEFFGK
EPRKDVNPDE AVAVGAAIQG QVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
TKFAQTFSTA EDNQPAVTIK VFQGEREIAS ANKLLGEFNL EGIPPASRGT PQIEVTFDID
ANGILHVGAK DKGTGKENKI TIKANSGLSE DEIQKMVKDA ELNAADDKKK LELVQARNQG
EAAVHTVTKS LSEHGDKLDA GEKEKIEAAV KDLEAALKTE DKAAIDEKTT ALMAASQKLG
EKMYGDAQAA QGAEAAGAQA AASGSAGAAA QDDNVVDAEV KEVKKG