ID   DNAK_WOLPP              Reviewed;         637 AA.
AC   B3CNB5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=WP0140;
OS   Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX   NCBI_TaxID=570417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=wPip;
RX   PubMed=18550617; DOI=10.1093/molbev/msn133;
RA   Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA   Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT   "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL   Mol. Biol. Evol. 25:1877-1887(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; AM999887; CAQ54248.1; -; Genomic_DNA.
DR   RefSeq; WP_012481744.1; NC_010981.1.
DR   AlphaFoldDB; B3CNB5; -.
DR   SMR; B3CNB5; -.
DR   STRING; 570417.WP0140; -.
DR   PRIDE; B3CNB5; -.
DR   EnsemblBacteria; CAQ54248; CAQ54248; WP0140.
DR   KEGG; wpi:WP0140; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_5; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008814; 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; 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..637
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119775"
FT   REGION          596..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..637
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   637 AA;  69052 MW;  0404540B06E45414 CRC64;
     MGRAIGIDLG TTNSCVAIMQ GKDAKVIENK EGARTTPSIV AFTSSGERLI GAPAKRQATT
     NANNTFFATK RLIGRQYSDP EMKNLGVPYK VFAAKNGDAW VKTTDGKEYS PSQIGAFILQ
     NLKEAAEAYL GEEVKDAVIT VPAYFNDSQR QATKDAGKIA GLNVLRIINE PTAAALAYGL
     DKKHGHTIVV YDLGGGTFDV SVLEIGDGVF EVKATNGDTH LGGEDFDNAV VNYLLGEFKK
     SNGIDLKNDP MAMQRIKEAA EKAKVELSSA METEVNLPFV TVDASGPKHL NIKLTRAKLE
     SLVNDLIERT IIPCKKALED AGLSASQIGE VVLVGGMTRM PKVIEKVKEF FGKDPHRGVN
     PDEVVAIGAA IQAGIIQGDV RDVLLLDVTP LSLGIETLGG VFTPLIERNT TIPTKKSQVF
     STAEDNQTAV TIKVHQGERK LAIDNKLLGQ FSLEGIPPAP RGVPQIEVTF DIDANGIAHV
     SAKDKATGKE QKIRIQSSGG LSEDEINRMV REAEEKAQED EKRKKFIEVK NQADSLVHST
     EKSLTEYGDK ISPEDKSAIE NAVNELKEVS KSDNIDDADS IQQKVTNLSQ LSMKLGEAMY
     KESQQQQGGE SSSTTNNEEE KVVDSDYQDM DNKEENK