DNAK_CLOB8
ID DNAK_CLOB8 Reviewed; 614 AA.
AC A6LRN4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Cbei_0830;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) 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; CP000721; ABR33014.1; -; Genomic_DNA.
DR RefSeq; WP_011968174.1; NC_009617.1.
DR AlphaFoldDB; A6LRN4; -.
DR SMR; A6LRN4; -.
DR STRING; 290402.Cbei_0830; -.
DR PRIDE; A6LRN4; -.
DR EnsemblBacteria; ABR33014; ABR33014; Cbei_0830.
DR GeneID; 66343771; -.
DR KEGG; cbe:Cbei_0830; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_9; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000000565; 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..614
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000079219"
FT REGION 577..614
FT /note="Disordered"
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 614 AA; 65342 MW; 332858618F533199 CRC64;
MGKIIGIDLG TTNSCVAVME GGEPTVIANS EGARTTPSVV SFQANGERLV GQVAKRQAIT
NPDKTVISIK RHMGTGYKVD IDGKQYSPQE ISAMVLQKIK ADAESYLGET VTQAVITVPA
YFNDSQRQAT KDAGKIAGLE VLRIINEPTA ASLAYGLDKT DSAHKILVYD LGGGTFDVSI
LDLGDGVFEV LSTNGDTKLG GDDFDEKIMK YIADEFKASN GIDLMQDKMA VQRLKEASEK
AKIELSASQQ TNINLPFITA DATGPKHIDL TLSRAKFNEI THDLVERSIE PMRKALADAK
LSLNDIDKII LVGGSTRIPA VVEAVKNFTG KEPSKGVNPD ECVAVGAAIQ AGVLTGEVKD
VVLLDVTPLT LGIETAGGIA TPLIERNTTI PTKKSQVFST AADNQTSVEI NVVQGERQMA
MDNKSLGQFT LSGIAPAPRG IPQIEVTFDI DANGIVKVSA LDKGTGKEAN ITITASTNLS
DDEVDKAVKE AEKFAEEDKK RKEKVEAVNN ADQTIYQIEK TLNEVGDKAT EDEKAAVRAK
IEDLKKVKDG DDVEATKAAI EAVNQSFYPI ATKMYQQAGG AEGAADPNAA AGGAQSAPHD
DNVVDADFKV DEDK