ID   DNAK_SINMW              Reviewed;         641 AA.
AC   A6UEY0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Smed_3389;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) 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; CP000738; ABR62210.1; -; Genomic_DNA.
DR   RefSeq; WP_012067591.1; NC_009636.1.
DR   RefSeq; YP_001329045.1; NC_009636.1.
DR   AlphaFoldDB; A6UEY0; -.
DR   SMR; A6UEY0; -.
DR   STRING; 366394.Smed_3389; -.
DR   PRIDE; A6UEY0; -.
DR   EnsemblBacteria; ABR62210; ABR62210; Smed_3389.
DR   GeneID; 61610940; -.
DR   KEGG; smd:Smed_3389; -.
DR   PATRIC; fig|366394.8.peg.6635; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001108; 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; 1.
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   Stress response.
FT   CHAIN           1..641
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059671"
FT   REGION          514..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   641 AA;  69023 MW;  2AF2F231766058D7 CRC64;
     MAKVIGIDLG TTNSCVSVMD GKDAKVIENA EGARTTPSMV AFTEDGERLV GQPAKRQAVT
     NPENTLFAIK RLIGRTFEDP TTQKDKGMVP YKIVKADNGD AWVEAHDKSY SPSQISAMIL
     QKMKETAESY LGEKVEKAVI TVPAYFNDAQ RQATKDAGKI AGLDVLRIIN EPTAAALAYG
     LDKKEGKTIA VYDLGGGTFD ISVLEIGDGV FEVKSTNGDT FLGGEDFDMR LVEYLASEFK
     KEQGIDLKND KLALQRLKEA AEKAKIELSS SQQTEINLPF ITADASGPKH LTMKLSRAKF
     ESLVDDLIQK TIAPCKAALK DAGVSAAEID EVVLVGGMTR MPKVQETVKQ LFGKEPHKGV
     NPDEVVAMGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRLIERN TTIPTKKSQV
     FSTADDNQSA VTIRVSQGER EMAADNKLLG QFDLVGIPPA PRGVPQIEVT FDIDANGIVQ
     VSAKDKGTGK EHQIRIQASG GLSDAEIEKM VKDAEANAEA DKKRREGVEA KNQAESLVHS
     SEKSLQEHGD KVSETDRKAI EDAIAALKSA VEASEPDAED IKAKTNTLME VSMKLGQAIY
     EAQQTESAHA DAAADAKRSG DDVVDADYEE VKDEDDRKRS A