ID   DNAK_TOLAT              Reviewed;         644 AA.
AC   C4L8Y5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=Tola_2257;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001616; ACQ93855.1; -; Genomic_DNA.
DR   RefSeq; WP_015879323.1; NC_012691.1.
DR   AlphaFoldDB; C4L8Y5; -.
DR   SMR; C4L8Y5; -.
DR   STRING; 595494.Tola_2257; -.
DR   PRIDE; C4L8Y5; -.
DR   EnsemblBacteria; ACQ93855; ACQ93855; Tola_2257.
DR   KEGG; tau:Tola_2257; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000009073; 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; 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..644
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205200"
FT   REGION          601..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..644
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   644 AA;  70175 MW;  ABBDEB97AD4BD4E1 CRC64;
     MGRIIGIDLG TTNSCVAILD GDTARVIENA EGDRTTPSII AYTDDGEILV GQPAKRQSIT
     NPKNTLYAIK RLIGRRYEDE EVQRDIKIMP FDIVRADNGD AWVDVKGRKL AAPQISAEVL
     KKMKKTAEDF LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAAFAYG
     VNKVQGERKI AVYDLGGGTF DISIIEIDEM DGEKTFEVLS TNGDTHLGGE DFDNRLINYL
     VDEFKREQGI DLRKDQLALQ RLKDSAEKAK IELSSAQQTE VNLPYITADA TGPKHMNIKV
     TRSKLESLVE DLVKKTIEPL KTALKDAGLS VSQLDDIILV GGQTRMPMVQ KAVADFFGKE
     PRKDVNPDEA VAMGAAIQGA VLAGEKHDVL LLDVTPLSLG IETMGSVMTT LIEKNTTIPT
     KKSQVFSTAD DNQSAVTIHV LQGERKRATD NKSLGQFNLE GIRPAPRGLP QIEVTFDIDA
     DGILHVSAKD KETGKEQNIT IQASSGLSDD EIQRMVREAE ANAAEDKKFE ELVQARNHAD
     ALIHATRKQI TEAGTALPAD EKAKIDAAVK ALEDALKSED KATIEAKQQE LMTASQKLME
     IAQQQAQQHQ HAHQGADAGA DTAGGKAHDD VVDAEFEEVK DDKK