ID   DNAK_RICPU              Reviewed;         627 AA.
AC   C4K110;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-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=RPR_02055;
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=562019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rustic;
RX   PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA   Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT   "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT   with virulent Rickettsia rickettsii: identification of virulence factors.";
RL   PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47261.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4K110; -.
DR   SMR; C4K110; -.
DR   EnsemblBacteria; ACR47261; ACR47261; RPR_02055.
DR   KEGG; rpk:RPR_02055; -.
DR   HOGENOM; CLU_005965_2_4_5; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000005015; 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_1000205197"
FT   REGION          598..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..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;  67920 MW;  4E6D483EE7D013F9 CRC64;
     MGKVIGIDLG TTNSCVAVME GKEPKVIENA EGERTTPSII AFANGEKLVG QSAKRQAVTN
     HRNTIYAVKR LIGRNFIDPM VKKDQGIVPY NIVKADNGDA WVEADNNKYS PSQISAFILQ
     KMKETAENYL GDKVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGF
     EKSASKTIAV YDLGGGTFDV SILEIADGVF EVKSTNGDTF LGGEDFDTRI LNHLIDVFKK
     ENGIDLSNDP LALQRLKEAA EKAKKELSSA VTTNINLPYI TADSSGPKHL NIKFTRAELE
     KLVDDLIEKT IEPCRKALQD AGFKASDIQE VVLVGGMTRM PKVQEAVKKF FGREPHKGVN
     PDEVVALGAA IQGGVLNKEV TDILLLDVTP LSLGIETLGG VFTRLIDRNT TIPTKKSQVF
     STADDNQHAV TIRVFQGERE MAKDNKLLGQ FNLEGIPLAP RGLPQIEVTF DIDANGIVHV
     SAKDKASGKE QKVTIQASGG LSDAEIEQMV KDAEQNADED KKRKELIEAK NAADSLVYST
     EKTLTEYGDK LSSDDKGAVE EALAALKAVL ESEDTALIKE KTESLTAASM KIGEAMYKAQ
     SESQPAAESA ANDEKIVDAD FQDVEKK