ID   DNAK_CORK4              Reviewed;         626 AA.
AC   C4LGV8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=ckrop_0278;
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=645127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717;
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(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; CP001620; ACR17063.1; -; Genomic_DNA.
DR   RefSeq; WP_012730951.1; NC_012704.1.
DR   AlphaFoldDB; C4LGV8; -.
DR   SMR; C4LGV8; -.
DR   STRING; 645127.ckrop_0278; -.
DR   PRIDE; C4LGV8; -.
DR   EnsemblBacteria; ACR17063; ACR17063; ckrop_0278.
DR   KEGG; ckp:ckrop_0278; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001473; 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..626
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205181"
FT   REGION          496..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..626
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   MOD_RES         176
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   626 AA;  67234 MW;  F9757DA801CB30DC CRC64;
     MGRAVGIDLG TTNSVVSVLE GGDPTVIANS EGSRTTPSVV AFSKNGEVLV GQSAKNQAVT
     NVDRTIRSVK RHIGDDSWNV DIDDKKYTAQ EISARILQKL KRDAESYLGE DVTDAVITVP
     AYFSDAQRQA TKDAGQIAGL NVLRIVNEPT AAALAYGLEK GEDDQTILVY DLGGGTFDVS
     LLEIGEGVVE VRATNGDNKL GGDDWDQRIV DWLTDKFKSS HGIDLTKDKM AMQRLREAAE
     KAKIELSSSQ QTSINLPYIT VDEDKNPLFL DETLSRTEFQ RITQDLLDRT RKPFQQVLSD
     AGISVSDIDH VVLVGGSTRM PAVTDLVKEL TGGKEPNKGV NPDEVVAVGA ALQAGVLRGE
     VKDVLLLDVT PLSLGIETKG GVMTKLIERN TTIPTKRSET FTTAEDNQPS VQIQVFQGER
     EMASANKLLG SFELGGIAPA PRGIPQIEVT FDIDANGIVH VTAKDKGTGK ENTIKIQDGS
     GLSQDEIDRM VKDAEAHAEE DKKRREEQEV RNSAESMVYQ TRKFVDDNKE KVSQDIQDKV
     EEAAKGVDEA LKGDDIEAIK SAVEKLSAES QEMGKSLYES EAANGGTTGG AAGAAGAAGA
     DAGSDNSDPN VVDAEVVDED KKDDDK