ID   DNAK_DESRM              Reviewed;         615 AA.
AC   A4J7F3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Dred_2496;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-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   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-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; CP000612; ABO51006.1; -; Genomic_DNA.
DR   RefSeq; WP_011878804.1; NC_009253.1.
DR   AlphaFoldDB; A4J7F3; -.
DR   SMR; A4J7F3; -.
DR   STRING; 349161.Dred_2496; -.
DR   PRIDE; A4J7F3; -.
DR   EnsemblBacteria; ABO51006; ABO51006; Dred_2496.
DR   KEGG; drm:Dred_2496; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001556; 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..615
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000072035"
FT   REGION          581..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   615 AA;  65530 MW;  D067A1407B322DBA CRC64;
     MGKVIGIDLG TTNSCVAVME GGEAVVIPNA EGARTTPSVV GFSKTGERLV GQVAKRQAVS
     NPDRTIQSIK RYMGTNHKVS IDGKDYSPQE ISAMILSKLK ADAEAYLGES VTQAVITVPA
     YFSDAQRQAT KDAGKIAGLE VLRIINEPTA AALAYGLDKE GDQTIQVFDL GGGTFDVSIL
     ELGDGVFEVK STSGNNRLGG DDFDQRIVDF LVAEFKKETG VDLSKDKMAM QRLKESAEKA
     KIELSGVLST NVNLPFISVG ADGPLHLDVN ISRAKFDELT ADLVEKTMGP TRQALADSGL
     ETNEINKVLM VGGSTRIPAV QEAVRKFLGK EPHKGINPDE CVALGAAIQA GVLAGEVKDV
     LLLDVTPLSL GIETLGGVFT KLIDRNTTIP TSKSQIFSTA ADNQPSVEIH VLQGERQMAA
     DNKTLGRFQL SGIPPAPRGV PQIEVKFDID VNGIVSVSAK DMGTGTVQSI SITGGTGGLS
     DDEINRMVNE AEKFAEEDKK RKEAVEVKNQ ADSLIYQAEK TIKDLGENAD KAKVEAVQKA
     VEELRTAMNG NDTDLIKNKL EELTKPLHEL TADLYQQQQA QQAAAQGGCA GGNCGGQAEK
     DNVVDADYEV KDDNK