DNAK_CLOBB
ID DNAK_CLOBB Reviewed; 616 AA.
AC B2TLZ7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=CLL_A0891;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-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}.
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DR EMBL; CP001056; ACD22007.1; -; Genomic_DNA.
DR RefSeq; WP_012422894.1; NC_018648.1.
DR AlphaFoldDB; B2TLZ7; -.
DR SMR; B2TLZ7; -.
DR PRIDE; B2TLZ7; -.
DR EnsemblBacteria; ACD22007; ACD22007; CLL_A0891.
DR KEGG; cbk:CLL_A0891; -.
DR PATRIC; fig|935198.13.peg.841; -.
DR HOGENOM; CLU_005965_2_1_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001195; 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..616
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000119689"
FT REGION 579..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..616
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 616 AA; 65842 MW; B522699D34792E75 CRC64;
MGKIIGIDLG TTNSCVAVME GGEPVVITNS EGARTTPSVV SFQADGERLV GQVAKRQSIT
NPDKTIISIK RHMGTSYKVD IDGKNYSPQE ISAMVLQKIK ADAESYLGES VTQAVITVPA
YFNDSERQAT KDAGKIAGLE VLRIINEPTA AALAYGLDKM DSNHKILVYD LGGGTFDVSI
LELGDGVFEV LSTNGDTKLG GDDFDQKVMD YIAETFKAEN GIDLRQDKMA LQRLKEAAEK
AKIELSSSMQ TNINLPFITA DATGPKHIDL NLTRAKFNEI TNDLVQRSIE PMKKALSDAA
ISIDEIEKII LVGGSTRIPA VVEAVKNFTG KDPSKGVNPD ECVAVGAAVQ AGVLTGEVKD
VLLLDVTPLT LGIETAGGIA TPLIERNTTI PTKKSQIFST AADSQTSVEI NVVQGERQMA
MDNKSLGRFT LSGIAPAPRG IPQIEVTFDI DANGIVKVSA LDKGTGKEAN ITITASTNLN
DDEIDKAVKE AEKFAEEDKK RKEKVETLNN ADQLIYQTEK ALTELGDKVS AEDKAKVTEK
LEALKAIKDG EDLEAIKKAT EELTQEFYAV SSKVYAAAGG DPSQAGGFDP NAAGGAQQEP
HDDNVVDADF KVDDDK