ID   DNAK_AERS4              Reviewed;         641 AA.
AC   A4SQ25;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=ASA_2996;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
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; CP000644; ABO90997.1; -; Genomic_DNA.
DR   RefSeq; WP_005312589.1; NC_009348.1.
DR   AlphaFoldDB; A4SQ25; -.
DR   SMR; A4SQ25; -.
DR   STRING; 382245.ASA_2996; -.
DR   PRIDE; A4SQ25; -.
DR   EnsemblBacteria; ABO90997; ABO90997; ASA_2996.
DR   KEGG; asa:ASA_2996; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000225; 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..641
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059502"
FT   REGION          600..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..624
FT                   /note="Polar 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   641 AA;  69557 MW;  EFA900D16A176129 CRC64;
     MGKIIGIDLG TTNSCVAILD GDTARVIENA EGDRTTPSII AYADDGEILV GQPAKRQAIT
     NPKNTLFAIK RLIGRRFEDE EVQRDLKIMP YAIAKADNGD AWVEVKGKKM APPQISAEVL
     KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAAFAYG
     VNKVKGERKV AVYDLGGGTF DISIIEIDEV EGETTFEVLA TNGNTHLGGE DFDNRVINYL
     VDEFKREQGI DLRNDQLALQ RLKDAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV
     TRAKLESLVE DMVKDSLEPV RTALKDSGLA VGEIDDVILV GGQTRMPMVQ KTVAEFFGKE
     PRKDVNPDEA VAMGAAIQGA VLSGEKTDVL LLDVTPLSLG IETMGSVMTA LIEKNTTIPT
     KKSQVFSTAE DNQSAVTIHV LQGERKRASD NKSLGQFNLE GIRPAQRGLP QIEVTFDIDA
     NGILHVSAKD KETNKEQKIT IQASSGLSDE EIERMVREAE ANAAEDKKFE ELVQTRNQAD
     GLVHSVRKQI TEAGDALPAD DKTKIETALS ELEAVIKGDD KAVIEAKQQA LLEASQKLME
     IAQQQSQAQG AGADANQSSS SSKADDDVVD AEFEEVKDDK K