ID   DNAK_BUCAP              Reviewed;         638 AA.
AC   Q8K9Y8;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 118.
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=BUsg_146;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE013218; AAM67714.1; -; Genomic_DNA.
DR   RefSeq; WP_011053681.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9Y8; -.
DR   SMR; Q8K9Y8; -.
DR   STRING; 198804.BUsg_146; -.
DR   GeneID; 75258977; -.
DR   KEGG; bas:BUsg_146; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   Proteomes; UP000000416; 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; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375:SF541; CHAPERONE PROTEIN DNAK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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_0000078434"
FT   REGION          600..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..638
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   638 AA;  70345 MW;  541CCFE2581F043F CRC64;
     MGKIIGIDLG TTNSCVAIMD GNKPRVLENS EGDRTTPSII AYTEKGEVLV GQPAKRQAIT
     NPKNTLFAIK RLIGRKFRDD EVQRDIKIMP YSIINSENGD AWIDVKKQKM APPQISAEVL
     KKMKKTAEDY LGESIKEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
     LDKGEGNRTI AVYDLGGGTF DISIIEIDDV DKEKTFEVLA TNGDTHLGGE DFDSRLINYL
     VQEFKKEQGI DLRNDSLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADS NGPKHLNIKV
     TRSKLESLVE DLVMRSIEPL KVALKDAGLS VGDINDVILV GGQTRMPMVQ SKVADFFGKE
     PRKDVNPDEA VAVGAAVQGG VLSGDVKDVL LLDVTPLSLG IETMGGIMTS LINKNTTIPT
     KHSQVFSTAE DNQSAVTIHI LQGERKRALD NKSLGQFNLD GIEPAPRGTA QIEVTFDIDS
     DGILHVSAKD KKTGKEQKIT IKASSGLNEE EIKKMINDAE ANSEADRKFE ELIQVRNQGD
     QLIHSIRKQL DENKNQIEKK ELEKIKSALD ELERSLKGEN KSEIEKNIQN LLNISSKLTE
     INQKKSEENL KKEDTSSESK KDENVVDAEF EEIKDPKK
//