ID   DNAK_CORU7              Reviewed;         617 AA.
AC   B1VHX4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=cu1815;
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=504474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109;
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
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; AM942444; CAQ05774.1; -; Genomic_DNA.
DR   RefSeq; WP_012361050.1; NC_010545.1.
DR   AlphaFoldDB; B1VHX4; -.
DR   SMR; B1VHX4; -.
DR   STRING; 504474.cu1815; -.
DR   PRIDE; B1VHX4; -.
DR   EnsemblBacteria; CAQ05774; CAQ05774; cu1815.
DR   GeneID; 60604598; -.
DR   KEGG; cur:cu1815; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001727; 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   Reference proteome; Stress response.
FT   CHAIN           1..617
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119692"
FT   REGION          496..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..617
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         176
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   617 AA;  66609 MW;  5FE3CB66E996C1D9 CRC64;
     MGRAVGIDLG TTNSVVSVLE GGEATVIANS EGARTTPSVV AFAKNGEVLV GQSAKNQAVT
     NVDRTISSVK RHIGNDSWNV EIDDKKYTAQ EISARTLMKL KRDAESYLGE DVTDAVITVP
     AYFNDSQRQA TKDAGQIAGL NVLRIVNEPT AAALAYGLEK GDKEQTILVF DLGGGTFDVS
     LLEIGDGVVE VRATSGDNKL GGDDWDQAIV DWLVEKFKNA NGIDLTKDKM ALQRLREAAE
     KAKIELSSSQ QASINLPYIT VDGDKNPLFL DETLSRTEFQ RITQDLLDRT KKPFQAVLKD
     ADVDINEIEH VVLVGGSTRM PAVTDLVKEL TGGKEPNKGV NPDEVVAVGA ALQAGVLRGE
     VKDVLLLDVT PLSLGIETKG GVMTKLIERN TTIPTKRSET FTTAEDNQPS VQIQVFQGER
     EMAQHNKLLG SFELGGIAPA PRGVPQIEVT FDIDANGIVH VTAKDKGTGK ENTIKIQDGS
     GLSQDEIDQM IKDAEAHAEE DKKRREEQEV RNSAESTVYQ TRKFVEDNKD KVSEDIQNKV
     EEAAKAVDEA LKGEDIEAIK DAMEKLSAES QEMGKAIYES EAAQAGEAGG AEDAGSEDPN
     VVDAEVVDED DSEDEKK