DNAK_MYCLB
ID DNAK_MYCLB Reviewed; 620 AA.
AC B8ZTB7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=MLBr02496;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=561304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Br4923;
RX PubMed=19881526; DOI=10.1038/ng.477;
RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA Rougemont J., Brennan P.J., Cole S.T.;
RT "Comparative genomic and phylogeographic analysis of Mycobacterium
RT leprae.";
RL Nat. Genet. 41:1282-1289(2009).
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; FM211192; CAR72595.1; -; Genomic_DNA.
DR RefSeq; WP_010908932.1; NC_011896.1.
DR AlphaFoldDB; B8ZTB7; -.
DR SMR; B8ZTB7; -.
DR EnsemblBacteria; CAR72595; CAR72595; MLBr02496.
DR KEGG; mlb:MLBr02496; -.
DR HOGENOM; CLU_005965_2_1_11; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000006900; 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..620
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000133156"
FT REGION 588..620
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 620 AA; 66679 MW; AFE89A7CD3B80D98 CRC64;
MARAVGIDLG TTNSVVSVLE GGDPVVVANS EGSRTTPSTV AFARNGEVLV GQPAKNQAVT
NVDRTIRSVK RHMGSDWSIE IDGKKYTAQE ISARVLMKLK RDAEAYLGED ITDAVITTPA
YFNDAQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLDKG EREQTILVFD LGGGTFDVSL
LEIGEGVVEV RATSGDNHLG GDDWDDRIVN WLVDKFKGTS GIDLTKDKMA MQRLREAAEK
AKIELSSSQS TSVNLPYITV DSDKNPLFLD EQLIRAEFQR ITQDLLDRTR QPFQSVVKDA
GISVSEIDHV VLVGGSTRMP AVTDLVKELT GGKEPNKGVN PDEVVAVGAA LQAGVLKGEV
KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTADDNQPSV QIQVYQGERE
IASHNKLLGS FELTGIPPAP RGVPQIEVTF DIDANGIVHV TAKDKGTGKE NTIKIQEGSG
LSKEEIDRMV KDAEAHAEED RKRREEADVR NQAETLVYQT EKFVKEQRET ENGSRVPEDT
LNKVEAAVAE AKTALGGTDI SAIKSAMEKL GQDSQALGQA IYEATQAASK VGGEASAPGG
SNSTDDVVDA EVVDDERESK