DNAK_MYCVP
ID DNAK_MYCVP Reviewed; 622 AA.
AC A1T2S3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Mvan_0634;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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; CP000511; ABM11473.1; -; Genomic_DNA.
DR RefSeq; WP_011777910.1; NC_008726.1.
DR AlphaFoldDB; A1T2S3; -.
DR SMR; A1T2S3; -.
DR STRING; 350058.Mvan_0634; -.
DR EnsemblBacteria; ABM11473; ABM11473; Mvan_0634.
DR KEGG; mva:Mvan_0634; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_11; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000009159; 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 Reference proteome; Stress response.
FT CHAIN 1..622
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059613"
FT REGION 588..622
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 622 AA; 66655 MW; B52B35A579D42D19 CRC64;
MARAVGIDLG TTNSVVAVLE GGDPVVVANS EGSRTTPSVV AFARNGEVLV GQPAKNQAVT
NVDRTIRSVK RHMGSDWTVK IDDKDYTPQE ISARVLMKLK RDAESYLGED ITDAVITVPA
YFNDAQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLDKG EKEQTILVFD LGGGTFDVSL
LEIGEGVVEV RATSGDNHLG GDDWDDRIVE WLVDKFKGTS GIDLTKDKMA MQRLREAAEK
AKIELSSSQS TSINLPYITV DADKNPLFLD EQLTRAEFQR ITQDLLDRTR KPFQQVIKDA
GIAVGDIDHV VLVGGSTRMP AVTELVKEMT GGQEPNKGVN PDEVVAVGAA LQAGVLKGEV
KDVLLLDVTP LSLGIETKGG VMTKLIERNT TIPTKRSETF TTADDNQPSV QIQVFQGERE
IAAHNKLLGS FELTGIPPAP RGVPQIEVTF DIDANGIVHV TAKDKGTGKE NTIKIQEGSG
LSKEEIDRMI KDAEAHADED RQRREEADVR NQAESLVYQT EKFVKEQREA EGGSKVPEDT
LTKVDSAIAD AKTALAGTDI GAIKSAMEKL GEESQALGQA IYEATQAEQA AGGAAGGDSA
GASGANDDVV DAEVVEDDQE RK