ID   DNAK_XYLFM              Reviewed;         638 AA.
AC   B0U3J8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, 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=Xfasm12_1512;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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; CP000941; ACA12427.1; -; Genomic_DNA.
DR   RefSeq; WP_004085852.1; NC_010513.1.
DR   AlphaFoldDB; B0U3J8; -.
DR   SMR; B0U3J8; -.
DR   PRIDE; B0U3J8; -.
DR   KEGG; xfm:Xfasm12_1512; -.
DR   HOGENOM; CLU_005965_2_1_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; 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..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119780"
FT   REGION          599..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   638 AA;  68460 MW;  7E48DB1DDD72524E CRC64;
     MGKIIGIDLG TTNSCLAIIE GGKGRVIENS EGDRTTPSIV AYTKDGEVLV GAAAKRQAVT
     NPKNTFYAVK RLIGRKFGDA EVQKDLDLVP YKITQHDNGD AWVATADGKK LAPQEISAKV
     LEKMKKTAED FLGEKVTEAV ITVPAYFNDS QRQATKDAGR IAGLDVKRII NEPTAAALAY
     GLDKKGGDRK IAVYDLGGGT FDVSIIEIAE VDGEKQFEVL ATNGDTFLGG EDFDKRVIDY
     LVDEFNKDQG IDLRKDPLAL QRLKDAAERA KIELSSSQQT EVNLPYITAD ASGPKHLNIK
     LTRAKLEALV DDLVRKSIEP CRIALNDAGL RTSDVQEVIL VGGQTRMPKV QQAVADFFGK
     EPRKDVNPDE AVALGAAIQG GVLAGDVKDV LLLDVTPLSL GIETMGGVFT KIIEKNTTIP
     TKASQVFSTA EDGQSAVTVH VLQGEREQAR FNKSLAKFDL AGIEPAPRGQ PQIEVSFDID
     ANGILHVSAK DKKTNKEQKV EVKAGSGLSD SEIQQMVADA EAHREEDKKF QELVQARNHA
     DGLIHSTRSA IKEHGSKVGG ELIGRVEASL AELEAAVKGD DKNQIEAKSK TLEEVAQSLH
     MAATAEQQSA STGAGAGSSA KVDDVVDAEF TEVKGDKK