DNAK_BACMK
ID DNAK_BACMK Reviewed; 611 AA.
AC A9VHU1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=BcerKBAB4_4165;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY45326.1; -; Genomic_DNA.
DR RefSeq; WP_002015198.1; NC_010184.1.
DR AlphaFoldDB; A9VHU1; -.
DR SMR; A9VHU1; -.
DR STRING; 315730.BcerKBAB4_4165; -.
DR EnsemblBacteria; ABY45326; ABY45326; BcerKBAB4_4165.
DR GeneID; 66266111; -.
DR KEGG; bwe:BcerKBAB4_4165; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000002154; 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; 2.
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..611
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119669"
FT REGION 579..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 611 AA; 65783 MW; BC2EEB16983F5ED4 CRC64;
MSKIIGIDLG TTNSCVAVME GGEPKVIPNP EGNRTTPSVV AFKNEERQVG EVAKRQAITN
PNTIMSVKRH MGTDYKVEVE GKDFTPQEIS AIILQNLKAS AEAYLGETVT KAVITVPAYF
NDAERQATKD AGRIAGLEVE RIINEPTAAA LAYGLEKQDE EQKILVYDLG GGTFDVSILE
LADGTFEVIS TAGDNRLGGD DFDQVIIDHL VAEFKKENSI DLSQDKMALQ RLKDAAEKAK
KDLSGVTQTQ ISLPFISAGA AGPLHLELTL TRAKFEEISA GLVERTLEPT RRALKDAGFA
PSELDKVILV GGSTRIPAVQ EAIKRETGKE PYKGVNPDEV VALGAAVQGG VLTGDVEGVL
LLDVTPLSLG IETMGGVFTK LIERNTTIPT SKSQVFSTAA DNQPAVDIHV LQGERPMSAD
NKTLGRFQLT DLPPAPRGIP QIEVTFDIDA NGIVNVRAKD LGTSKEQTIT IQSSSGLSDE
EVDRMVQEAE SNADADQKRK EEVELRNEAD QLVFQTDKVV KDLEGKVDAA EVAKATEAKE
ALQAAIEKNE LEEIRVKKDA LQEIVQQLTV KLYEQAQAAA GQAEGAQGAQ DAGAKKDNVV
DAEFEEVKED K