ID   DNAK_RICPR              Reviewed;         627 AA.
AC   Q9ZDX9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=RP185;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AJ235270; CAA14651.1; -; Genomic_DNA.
DR   PIR; D71729; D71729.
DR   RefSeq; NP_220574.1; NC_000963.1.
DR   RefSeq; WP_004595925.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDX9; -.
DR   SMR; Q9ZDX9; -.
DR   STRING; 272947.RP185; -.
DR   EnsemblBacteria; CAA14651; CAA14651; CAA14651.
DR   GeneID; 57569313; -.
DR   KEGG; rpr:RP185; -.
DR   PATRIC; fig|272947.5.peg.192; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002480; 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   Reference proteome; Stress response.
FT   CHAIN           1..627
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078530"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   627 AA;  68383 MW;  A638A0A5A5C8ACC7 CRC64;
     MGKVIGIDLG TTNSCVAVME GKEPKVIDNA EGERTTPSII AFANSERLVG QPAKRQAVTN
     PRNTIYAVKR LIGRNFTDPM VRKDQGLVPY NIVKADNGDA WVEADNHKYS PSQISAFILQ
     KMKETAENYL GEKVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGF
     EKSSSKTIAV YDLGGGTFDV SILEISDGVF EVKSTNGDTF LGGEDFDTRI LNHLIEVFKK
     ESGIDLSKDP LALQRLKEAA EKAKKELSST STTDINLPYI TADSTGPKHL NIKFTRAELE
     KLVDDLIEKT IEPCRQALKD AGFKPNDIQE VVLVGGMTRM PKVQEAVKKF FGREPHKGVN
     PDEVVALGAA IQGGVLNKEV TDILLLDVTP LSLGIETLGG VFTRLIDRNT TIPSKKSQVF
     STADDNQHAV TIRVFQGERE MAKDNKLLGQ FNLEGIPPAP RGVPQIEVTF DIDANGIVHV
     SAKDKASGKE QKVTIQASGG LSDAEIEQMV KDAEHNADED KKRKELIETK NAADSLVYST
     EKTLREYGDK LSSEEKGTVE EALTSLKAAL ESEDASLIKE KTGNLTAANM KIGEAMYKTQ
     TENQHSEANT VNNEKVVDAD FQDVDKK