DNAK_CLOBJ
ID DNAK_CLOBJ Reviewed; 623 AA.
AC C1FVU0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=CLM_3354;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001581; ACO85670.1; -; Genomic_DNA.
DR RefSeq; WP_003357980.1; NC_012563.1.
DR AlphaFoldDB; C1FVU0; -.
DR SMR; C1FVU0; -.
DR STRING; 536232.CLM_3354; -.
DR EnsemblBacteria; ACO85670; ACO85670; CLM_3354.
DR GeneID; 5184256; -.
DR KEGG; cby:CLM_3354; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000001374; 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; 2.
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..623
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133138"
FT REGION 580..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 623 AA; 66832 MW; 9328C79FF262D23E CRC64;
MAKIIGIDLG TTNSCVSVME GGEPVVIPNA EGSRTTPSVV SFQANGERLI GQVAKRQAIT
NPEKTIISIK RYMGTDHKVN IDSTEYTPQQ ISAMVLQKLK ADAEAYLGEK VTQAVITVPA
YFNDSQRQAT KDAGKIAGLE VLRIINEPTA ASLAYGLDKM DTNEKILVYD LGGGTFDVSI
LELGDGVFEV KATNGDTKLG GDDFDQKLID YIAETFKAEN GIDLRNDKMA IQRLKEAAEK
AKIELSSATQ TNINLPFITA DATGPKHIDM NLTRAKFNEL THDLVQRTLE PIKKSLEGSG
YAMSDIDKII MVGGSTRIPA VQDAVKDFTG KELSKGVNPD EVVAMGAAIQ AGVLTGEVKD
VLLLDVTPLT LGIETFGGVS TTLIEKNTTI PTRKSQVFST AADGQTSVEI HVVQGERSMA
ADNKTLGRFT LSGIAPAPRG IPQIEVTFDI DANGIVNVSA KDKGTGKEAN ITITASTNLT
DDEIEKAVNE AKKFEAEDKK RKESIEIKNN ADQIVYQTEK TLTDLGDKVS AEDKAQIEEK
VKAVKDVKDG EDLEAIKKAT EDLTQTFYGI SSKIYQQANP EGAQGAGFDP NNMGGANAGN
ASAGNDKKDD NVVDADFKVE DDK