DNAK_CLOBM
ID DNAK_CLOBM Reviewed; 623 AA.
AC B1KZN7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=CLK_2344;
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA55690.1; -; Genomic_DNA.
DR RefSeq; WP_012343643.1; NC_010520.1.
DR AlphaFoldDB; B1KZN7; -.
DR SMR; B1KZN7; -.
DR EnsemblBacteria; ACA55690; ACA55690; CLK_2344.
DR KEGG; cbl:CLK_2344; -.
DR HOGENOM; CLU_005965_2_4_9; -.
DR OMA; ISIKRHM; -.
DR Proteomes; UP000000722; 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_1000119691"
FT REGION 580..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..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; 66863 MW; 351DBA8EBA2AF0A6 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 RKESIEVKNN ADQIVYQTEK TLTDLGDKVS AEDKATIEEK
VKAVKDVKEG EDLEAIKKAT EDLTQTFYGI SSKIYQQANP EGAQGAGFDP NNMGGANADN
ASAGNDKKDD NVVDADFKVE DDK