ID   DNAK_EHRCJ              Reviewed;         634 AA.
AC   Q3YRR6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Ecaj_0554;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake;
RX   PubMed=16707693; DOI=10.1128/jb.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68589.1; -; Genomic_DNA.
DR   RefSeq; WP_011304667.1; NC_007354.1.
DR   AlphaFoldDB; Q3YRR6; -.
DR   SMR; Q3YRR6; -.
DR   STRING; 269484.Ecaj_0554; -.
DR   PRIDE; Q3YRR6; -.
DR   EnsemblBacteria; AAZ68589; AAZ68589; Ecaj_0554.
DR   KEGG; ecn:Ecaj_0554; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000435; 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..634
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000225961"
FT   REGION          597..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         193
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   634 AA;  68963 MW;  B929AC51BF655422 CRC64;
     MAVIGIDLGT TNSCVAVMEG GDAKAIENSE GARTTPSIVA FTDSERLVGD PAKRQATTNA
     KNTIYASKRL IGRRYQDVKD IKSSYEVVSA KNGDAWIKVL GKEYSPSQIG AFVLEKMKET
     AERHLGHKVE KAVITVPAYF NDAQRQATKD AGKIAGLDVI RIINEPTAAA LAYGLNKSDK
     QKVIAVYDLG GGTFDVSILE IADGVFEVKA TNGDTMLGGE DFDHAIMDYL MDDFKKTTGI
     DLHNDAMAVQ RIKEASEKAK IELSNRMETD INLPFISSDS TGPKHLSLKL TRAKFENLVD
     DLIQRTIEPC KKALKDAGIS ADKIDEVVLV GGMTRVPKVI QKVKEFFGRE PHKGVNPDEV
     VAIGAAIQGS ILAGDVRDVL LLDVTPLSLG IETLGGVFTP LIERNTTIPT KKSQVFSTAE
     DGQTAVTIKV YQGERKMAAD NKLLGQFSLE GIPSAPRGMP QIEVTFDIDA NGIVHVSAKD
     KASGKEQAIK IQSSGGLSDD EIQRMIKEAE QKAGEDEKRK KFIELKNNGE NLVHSTEKSL
     NEYGDKIPNS DRLEIENAIR DVRDALGNSD VESVDILQQK VDHLMKVSMK LGEALYGNAN
     NTSSTESTTT NNNNEEDSKV VDSDYQEIDK KDGK