ID   DNAK_XANCB              Reviewed;         642 AA.
AC   B0RVU2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=xcc-b100_2799;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(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; AM920689; CAP52160.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RVU2; -.
DR   SMR; B0RVU2; -.
DR   PRIDE; B0RVU2; -.
DR   KEGG; xca:xcc-b100_2799; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001188; 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..642
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119776"
FT   REGION          603..627
FT                   /note="Disordered"
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   642 AA;  68837 MW;  404DE445E1EA364C CRC64;
     MGKIIGIDLG TTNSCVAIMD GGKARVIENS EGDRTTPSIV AYTKDGEVLV GASAKRQAVT
     NPKNTFYAVK RLIGRKFTDG EVQKDISHVP YGILAHDNGD AWVQTSDSKR MAPQEISARV
     LEKMKKTAED FLGEKVTEAV ITVPAYFNDS QRQATKDAGR IAGLDVKRII NEPTAAALAY
     GLDKNGGDRK IAVYDLGGGT FDVSIIEIAE VDGEKQFEVL ATNGDTFLGG EDFDNRVIEY
     LVDEFNKDQG IDLRKDPLAL QRLKDAAERA KIELSTSQQT EVNLPYVTAD ASGPKHLNIK
     LTRAKLEALV EDLVKKSIEP CRTALNDAGL RASDINEVIL VGGQTRMPKV QQAVADFFGK
     EPRKDVNPDE AVAVGAAIQG GVLAGDVKDV LLLDVTPLSL GIETMGGVFT KIIEKNTTIP
     TKASQTFSTA EDNQSAVTVH VLQGEREQAR FNKSLAKFDL SGIEPAPRGM PQVEVSFDID
     ANGILHVSAK DKKTNKEQKV EIKAGSGLSD EEIQRMVADA EANREEDKKF QELVQTRNQA
     DGLIHATRTA ITEHGSKVGG DVIGKVEAAL ADLETAMKGD DKAQIEARSK TLEEAGQSLY
     AAAAAAEQGG NADAASGNAQ ASKAADDVVD AEFTEVKDDK KA