ID   DNAK_RICTY              Reviewed;         627 AA.
AC   Q68XI2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=RT0176;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03660.1; -; Genomic_DNA.
DR   RefSeq; WP_011190647.1; NC_006142.1.
DR   AlphaFoldDB; Q68XI2; -.
DR   SMR; Q68XI2; -.
DR   STRING; 257363.RT0176; -.
DR   EnsemblBacteria; AAU03660; AAU03660; RT0176.
DR   KEGG; rty:RT0176; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000604; 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..627
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000226005"
FT   REGION          602..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..627
FT                   /note="Basic and acidic residues"
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   627 AA;  68319 MW;  C03595F8EB031231 CRC64;
     MGKVIGIDLG TTNSCVAVME GKEPKVIDNA EGERTTPSII AFANSERLVG QPAKRQAVTN
     PRNTIYAVKR LIGRNFTDPM VRKDQGLVPY NIVKADNGDA WVEADNNKYS PSQISAFILQ
     KMKETAENYL GEKVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGF
     EKSSSKTIAV YDLGGGTFDV SILEISDGVF EVKSTNGDTF LGGEDFDTRI LNHLIDVFKK
     DSGIDLSKDP LALQRLKEAA EKAKKELSST SATDINLPYI TADSTGPKHL NIKFTRAELE
     KLVDDLIEKT IEPCRQALKD AGFKPTDIQE VVLVGGMTRM PKVQEAVKKF FGREPHKGVN
     PDEVVALGAA IQGGVLNKEV TDILLLDVTP LSLGIETLGG VFTRLIDRNT TIPSKKSQVF
     STADDNQHAV TIRVFQGERE MAKDNKLLGQ FNLEGIPPAP RGVPQIEVTF DIDANGIVHV
     SAKDKASGKE QKVTIQASGG LSDSEIEQMV KDAEHNADED KKRKELIETK NAADSLVYST
     EKTLREYGDK LSSEEKGAVE EALASLKSAL ESEDASLIKE KTNNLTAANM KIGETMYKAQ
     TENQHSEANT VNDEKVVDAD FQDVDKK