DNAK_BURVG
ID DNAK_BURVG Reviewed; 650 AA.
AC A4JBS1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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};
GN OrderedLocusNames=Bcep1808_0712;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-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; CP000614; ABO53724.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JBS1; -.
DR SMR; A4JBS1; -.
DR STRING; 269482.Bcep1808_0712; -.
DR EnsemblBacteria; ABO53724; ABO53724; Bcep1808_0712.
DR KEGG; bvi:Bcep1808_0712; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000002287; Chromosome 1.
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..650
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059526"
FT REGION 613..634
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 650 AA; 69829 MW; D8E2446B2EBFBA48 CRC64;
MGKIIGIDLG TTNSCVAIME GNQVKVIENS EGARTTPSII AYMDDNEVLV GAPAKRQSVT
NPKNTLFAVK RLIGRRFEEK EVQKDIGLMP YAIIKADNGD AWVEAHGEKL APPQISAEVL
RKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAFG
LDKAEKGDRK IAVYDLGGGT FDVSIIEIAD VDGEMQFEVL STNGDTFLGG EDFDQRIIDY
IIGEFKKEQG VDLSKDVLAL QRLKEAAEKA KIELSSSQQT EINLPYITAD ASGPKHLNLK
ITRAKLEALV EDLVERTIEP CRIAIKDAGV KVSDIDDVIL VGGQTRMPKV QEKVKEFFGK
EPRRDVNPDE AVAVGAAIQG QVLSGDRKDV LLLDVTPLSL GIETLGGVMT KMITKNTTIP
TKHSQVYSTA DDNQSAVTIK VFQGEREMAA GNKLLGEFNL EGIPPAPRGV PQIEVTFDID
ANGILHVGAK DKATGKENKI TIKANSGLSD AEIDQMIKDA EANAAEDHKL RELADSRNQG
DALVHSTKKA LTEYGDKLDA GEKEKIEAAL KSLEDVLKDT SADKAAIDAK VEELGKASQK
LGEKMYADMQ AQQAGAAGAA GAAEGAAHAG GAQQAADDVV DAEFKEVKKD