ID   DNAK_NEOSE              Reviewed;         636 AA.
AC   O85282;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
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;
OS   Neorickettsia sennetsu (Ehrlichia sennetsu).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Japan;
RX   PubMed=9632573; DOI=10.1128/iai.66.7.3106-3112.1998;
RA   Zhang Y., Ohashi N., Rikihisa Y.;
RT   "Cloning of the heat shock protein 70 (HSP70) gene of Ehrlichia sennetsu
RT   and differential expression of HSP70 and HSP60 mRNA after temperature
RT   upshift.";
RL   Infect. Immun. 66:3106-3112(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; AF060197; AAC27487.1; -; Genomic_DNA.
DR   AlphaFoldDB; O85282; -.
DR   SMR; O85282; -.
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..636
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078461"
FT   REGION          514..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..636
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:0000250"
SQ   SEQUENCE   636 AA;  68358 MW;  12A9F79C00473676 CRC64;
     MAGEIAIGID LGTTNSCVAI KDKVIENAEG ARTTPSVVAF TSDGQTLVGA PAQRQAVTNA
     KNTIVASKRL IGRRFKDNVI KGIQKDYPYK IVEAKNGDAW IEAGGKSYSP SQVGANVLIK
     LKEAAETYTG KKVTKAVITV PAYFDDAQRT ATKDAGRIAG LEVLRIINEP TAAALAYGLD
     KTATTKNIAV FDLGGGTFDV SILELGDGVF EVKATNGDTH LGGEDFDRMI LNFLVEEFKK
     ENGMDLKNDP LALQRLKEAA EKAKKELSST QETDINLPYI TADAAGPKHL NVKFTRAKLE
     SLVSDLIDRT IEPCKKALKD SGLKREEINE VVLVGGMTRM PAVVKKVTEF FGKEPHKGVN
     PDEVVAIGAA IQANILAGGS DAQDIVLLDV TPLSLGIETL GGVFTKLIDR NTTIPTKRSQ
     TFSTAEDNQS AVTIRVFQGE RQMASDNKLL GQFSLGGIPP APRGMPQIEV TFDIDANGIV
     HVSAKDKGTG KEQTVKIQAS GGLTEEEIKK MVDEAASKAD EDKKRRELVE AKNSAESLIH
     STEKSLSEYG SKISSSDKQS IDDAISDLKS VLAKDDASLI KEKTDALSKV SMKLGEAMYK
     ESQSASNDSS PKNDSTEEGE RVVDPEYEEV KDEDSK