ID   DNAK_CLAMS              Reviewed;         623 AA.
AC   B0RBI1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=CMS2806;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX   PubMed=18192393; DOI=10.1128/jb.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(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; AM849034; CAQ02877.1; -; Genomic_DNA.
DR   RefSeq; WP_012300036.1; NZ_MZMN01000003.1.
DR   AlphaFoldDB; B0RBI1; -.
DR   SMR; B0RBI1; -.
DR   STRING; 31964.CMS2806; -.
DR   PRIDE; B0RBI1; -.
DR   EnsemblBacteria; CAQ02877; CAQ02877; CMS2806.
DR   KEGG; cms:CMS2806; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001318; 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..623
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000079218"
FT   REGION          581..623
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   623 AA;  67123 MW;  CB678AA787658A20 CRC64;
     MARAVGIDLG TTNSVVSVLE GGEPTVIANA EGARTTPSVV AFTKDGEVLV GETAKRQNVT
     NVDRTISSVK RHMGTDWTVG IDDKKYTSQE LSARILGKLK RDAEQYLGDS VTDAVITVPA
     YFNDAERQAT KEAGEIAGLN VLRIINEPTA AALAYGLDRG KEDELILVFD LGGGTFDVSL
     LEVGKDDDFS TIQVRSTAGD NRLGGDDWDQ RIVDHLVKRF KESTGVDVSN DKIAKQRLKE
     AAEQAKKELS SSTSTSIQLP YLSLTENGPA NLDETLTRAK FEELTNDLLE RTRKPFEDVI
     REAGVSVGDV AHVVLVGGST RMPAVVDLVK KLTGGKEPNK GVNPDEVVAV GAALQAGVLK
     GERKDVLLID VTPLSLGIET KGGIMTKLIE RNTAIPTKRS ETFTTADDNQ PSVAIQVFQG
     EREFTRDNKN LGTFELTGIA PAPRGIPQVE VTFDIDANGI VHVSAKDKGT GKEQSMTITG
     GSSLAKEDIE RMVREAEEHA AEDKTRREQA EVRNNAEQLA YSIDKLIKEN DDKLPEDVKS
     EVQGDVDGLK SALAGDDETA VKTAFDKLSA SQTKLGEAIY AQGQQEQAAG EAPEGASEAK
     KDDEDIVDAE VVDEDDEDKK TDR