ID   DNAK_PSYWF              Reviewed;         641 AA.
AC   A5WI20;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=PsycPRwf_2371;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) 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; CP000713; ABQ95311.1; -; Genomic_DNA.
DR   RefSeq; WP_011961582.1; NC_009524.1.
DR   AlphaFoldDB; A5WI20; -.
DR   SMR; A5WI20; -.
DR   STRING; 349106.PsycPRwf_2371; -.
DR   PRIDE; A5WI20; -.
DR   EnsemblBacteria; ABQ95311; ABQ95311; PsycPRwf_2371.
DR   KEGG; prw:PsycPRwf_2371; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
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_1000072040"
FT   REGION          605..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   641 AA;  69023 MW;  779657DB2CAD8C48 CRC64;
     MAKTIGIDLG TTNSCVAVME GDKVKVIENA EGTRTTPSII AYKDGEILVG QSAKRQAVTN
     PNNTLYAIKR LIGRRFDDKV VQKDIGMVPY KIVKADNGDA WVEVNDKKMA PPQISAEILQ
     KMKKTAEDYL GEKVTDAVVT VPAYFNDSQR QATKDAGKIA GLNVKRIINE PTAAALAYGM
     DKKKGDSTVA VYDLGGGTFD VSIIEIADVD GEQQFEVLST NGDTFLGGED FDLALIDYLV
     EEFKKEQNFN LKGDPLAMQR LKEAAEKAKI ELSSAQSTEV NLPYITADAS GPKHLVVTIS
     RSKLEALTEA LVKRTIDPCK VALEDAGLKA SDIDDVILVG GQTRMPLVQK TVEEFFGQEP
     RKDVNPDEAV AVGAAIQGAV LSGDKTDVLL LDVTPLTLGI ETMGGVMTGI IEKNTMIPTK
     KSQVFSTAED NQPAVTIKVF QGERKVAAQN KLLGEFNLTD IPPAPRGMPQ IEVTFDINAD
     GIMNISAKDK GTGKEQSIQI KADSGLSDEE IEQMVRDAEA NAAEDEKFAA LAQVRNEADG
     RIHAIQKALK DAEDKVTEEE KSSVETAISD LELAAKEDDH DDIKAKLEAL DNAFLPISQK
     IYAAGQGAEG AAPQADATEA NAADDDVVDA EFTEVNEDDK K