ID   DNAK_XYLF2              Reviewed;         638 AA.
AC   B2I6F6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=XfasM23_1455;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
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; CP001011; ACB92866.1; -; Genomic_DNA.
DR   RefSeq; WP_004091050.1; NC_010577.1.
DR   AlphaFoldDB; B2I6F6; -.
DR   SMR; B2I6F6; -.
DR   EnsemblBacteria; ACB92866; ACB92866; XfasM23_1455.
DR   GeneID; 58016894; -.
DR   KEGG; xfn:XfasM23_1455; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001698; 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   Stress response.
FT   CHAIN           1..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119779"
FT   REGION          598..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..615
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;  68444 MW;  7E48DB186513D44E 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
     MAATAEQQSG STGAGAGASA KVDDVVDAEF TEVKADKK