ID   DNAK_DESDA              Reviewed;         638 AA.
AC   B8J402;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Ddes_2151;
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 / DSM 6949 / MB;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) 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; CP001358; ACL50047.1; -; Genomic_DNA.
DR   RefSeq; WP_015939156.1; NC_011883.1.
DR   AlphaFoldDB; B8J402; -.
DR   SMR; B8J402; -.
DR   STRING; 525146.Ddes_2151; -.
DR   EnsemblBacteria; ACL50047; ACL50047; Ddes_2151.
DR   KEGG; dds:Ddes_2151; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_7; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000133142"
FT   REGION          597..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   638 AA;  68385 MW;  87C5AF6E3D6B962A CRC64;
     MSKIIGIDLG TTNSCVYVME GKDPKCITNP EGGRTTPSVV AFTDKERLVG EIAKRQAVTN
     PTRTIFAIKR LMGRKFDSPE VDRWKEHSPY AIVKAPNGDA GVEVDGRTYS SPEISAMILA
     KLKADAEAYL GETVTEAVIT VPAYFNDAQR QATKDAGRIA GLEVKRIINE PTAASLAYGA
     DKKANEKIAV FDLGGGTFDI SILEVGDNVV EVRATNGDTF LGGEDFDQRV INFLVEEFKK
     ENGIDLSKDS MALQRLKEAA EKAKKDLSTS METEVNLPFI TADQNGPKHM LVKISRAKLE
     SLVGDLVEST TEPCKKALAD AGMTADQIDE VILVGGMTRM PLVQQVVGKF FGKEPNRSVN
     PDEVVAMGAA IQGGILSGDV KDVLLLDVTP LSLGIETMGG VFTRLIERNT TIPTRKSQVF
     TTASDNQPSV SIHVLQGERP MSADNMTLAR FDLAGIPPAP RGVPQIEVSF DIDANGIVNV
     SAKDMGTGKE QSIKITASSG LSEEDIQKLV REAEAHATDD KKKQELIEAR NHADSLIYGT
     EKSLADLGDK ADAAVKSDIE TKMADLRKLM EGEDAAAIKT ATDELAKASH KLAEQLYQQQ
     AQQTGAAGAQ ADAGAAEGQP QGNAADDVVD ADYTEVKK