ID   DNAK_WIGBR              Reviewed;         645 AA.
AC   Q8D2Q5;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=WIGBR2990;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24445.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8D2Q5; -.
DR   SMR; Q8D2Q5; -.
DR   STRING; 36870.25166255; -.
DR   PRIDE; Q8D2Q5; -.
DR   EnsemblBacteria; BAC24445; BAC24445; BAC24445.
DR   KEGG; wbr:dnaK; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000562; 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   Reference proteome; Stress response.
FT   CHAIN           1..645
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078587"
FT   MOD_RES         203
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   645 AA;  71392 MW;  D935BA4D054B8AE8 CRC64;
     MEILMGNIIG IDLGTTNSCV AIIENGKVKV IENSEGDRTT PSIIAYTEEN EILVGQPAKR
     QSVTNPKNTF FAIKRLIGRK FTDHEVQRDV NIMPYKIVSS ENGDVWLNVK NQKVAPPQIS
     AEILKKMKKT AEDYIGKSIT EAVITVPAYF NDTQRQATKD AGKIAGLDVK RIINEPTAAA
     LAYGLDKKTG NRIIAVYDLG GGTFDISIIE IDDVDGEKTF EVLSTNGDTH LGGEDFDSRL
     INYLVNEFKK EQGIDLRNDP LAMQRLKESS EKAKIELSSV HQTDVNLPYI TADSSGPKHM
     NIKVTRAKLE SLVEELIYKT LEPVKTSLKD AKLKIIDIKD VILVGGQTRM PLVQKKVSDF
     FGKEPRKDVN PDEAVAIGAA VQGGVLAGDV KDVLLLDVTP LSLGIETMGG VMTTLISKNT
     TIPTKHSQIF STAEDNQSAV TIHVLQGERK RSIDNKSLGQ FNLDGIAPAM RGMPQIEVTF
     DIDADGILHV SAKDKNSGRE QKITIKASSG LSENEIDKML KESEANAELD IKFEELVKTK
     NQADHLLHST RKQIKEAKNL PLEKKTEIEK CINELELSIK GEDKKDIEIK IQSLIQISSC
     LVDFSKNKEN LNKEDIIKTN KKENNNKTND DVVDAEFEEI KDKKN