DNAK_VEREI
ID DNAK_VEREI Reviewed; 653 AA.
AC A1WGJ9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Veis_0979;
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2;
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 Verminephrobacter eiseniae EF01-2.";
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; CP000542; ABM56756.1; -; Genomic_DNA.
DR RefSeq; WP_011808769.1; NC_008786.1.
DR AlphaFoldDB; A1WGJ9; -.
DR SMR; A1WGJ9; -.
DR STRING; 391735.Veis_0979; -.
DR PRIDE; A1WGJ9; -.
DR EnsemblBacteria; ABM56756; ABM56756; Veis_0979.
DR KEGG; vei:Veis_0979; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000374; 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..653
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059695"
FT REGION 607..653
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 653 AA; 69588 MW; 580803497F2887D1 CRC64;
MGRIIGIDLG TTNSCVSIME GNTTRVIENS EGARTTPSIV AYQEDGEILV GASAKRQAVT
NPKNTLYAVK RLIGRKFTEK EVQKDIDLMP YKIVAAENGD AWIEVRGTKL SAQQVSADIL
RKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
LDKQEKGDRK IAVYDLGGGT FDVSIIEIAD VDGEKQFEVL STNGDTFLGG EDFDQRIIDY
IISEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSNSAAT DINLPYITAD ASGPRHLSIK
LTRAKLESLV DELIERTIAP CRMAIKDAGV SVSDIHDVIL VGGMTRMPKV QEMVKEFFGK
DPRKDVNPDE AVAVGAAIQG QVLTGERKDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
TKFAQTFSTA DDNQPAVTIK VFQGEREMAS GNKLLGEFNL EGIPPAARGV PQIEVSFDID
ANGILHVGAK DKGTGKENKI TIKANSGLSE EEIQQMIKDA ELNAADDKRK LELVQVRNQA
EAAVHSVTKN LAEHGDKLDA GEKDAIAAAV KALEEALKGE DKAAIADKTT ALMAASQKLG
EKMYAESQAA QAAQGAAAGA GNAGGAGGAS DASGKPAGDD NVVDAEVKEV KKG