DNAK_BDEBA
ID DNAK_BDEBA Reviewed; 637 AA.
AC Q6MNF8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Bd1298;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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; BX842649; CAE79194.1; -; Genomic_DNA.
DR RefSeq; WP_011163796.1; NC_005363.1.
DR AlphaFoldDB; Q6MNF8; -.
DR SMR; Q6MNF8; -.
DR STRING; 264462.Bd1298; -.
DR PRIDE; Q6MNF8; -.
DR EnsemblBacteria; CAE79194; CAE79194; Bd1298.
DR KEGG; bba:Bd1298; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_7; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000008080; 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..637
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225940"
FT REGION 596..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 637 AA; 68382 MW; A5B9E82003056FF6 CRC64;
MGKIIGIDLG TTNSCVAIME GGEPKVLVNE EGARTTPSVV AYTKDGDRLV GQIAKRQAVT
NPENTIYSAK RFIGRRFEEI QEEIKLVPYT VVAKGNDCAF KVQGKTASPE EIGAAVLAKL
KKVAEDYLGE PVTEAVVTVP AYFNDAQRQA TKDAGRIAGL EVKRIINEPT AAALAYGMDK
KKDEKIVIYD FGGGTFDVSI LEVGDGVVEV RATNGDTHLG GDNFDTVILE WLITEFKKDQ
AIDLKNDKMA LQRLKEAAEK AKIELSSAQE TEINLPFITA DQSGPKHLQT RLSRAKFDQM
TEDLVKRSME PCRKALADSG LKASEIDEVV LVGGSTRIPA IQKAVKDFFG KEPNRSVNPD
EVVAIGAAVQ GGVLAGDVKD VLLLDVTPLS LGIETLGGVM TTLIERNTAI PSKKSQVFST
AADNQPAVDI HVLQGERKMA GDNKTLGRFE LVGIPPAPRG VPQVEVTFDI DANGILHVSA
KDMSSGKSQQ IKITAQSGMS EDEIKRAVAD AEGHAEEDKR KAEAATQRNN LDNLVYQTEK
LIKDSGAQLP ESEVKSANEA VAEAKKILEN KSASGDELKG AFERLQNLTH KLTSELYKKQ
GAQPGAEGQQ ADAAEGGEAS ANKGGDDVID ADYKDVN