ID   DNAK_BUCBP              Reviewed;         638 AA.
AC   P59565;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=bbp_142;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26876.1; -; Genomic_DNA.
DR   RefSeq; WP_011091277.1; NC_004545.1.
DR   AlphaFoldDB; P59565; -.
DR   SMR; P59565; -.
DR   STRING; 224915.bbp_142; -.
DR   PRIDE; P59565; -.
DR   EnsemblBacteria; AAO26876; AAO26876; bbp_142.
DR   GeneID; 56470686; -.
DR   KEGG; bab:bbp_142; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000601; 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   Reference proteome; Stress response.
FT   CHAIN           1..638
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078435"
FT   REGION          598..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..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;  70368 MW;  9C4F87571EE0AD82 CRC64;
     MSKIIGIDLG TTNSCIAIMD GNKARVLENS EGDRTTPSII AYTNDNEILI GKPAKRQSIT
     NPKNTLFAIK RLIGRKFTDN EVQRDIKIMP YKIIQSENGD AWINIKNKKL APPQISAEIL
     KKMKKTAEDY LGESIQEAVI TVPAYFNDAQ RQATKDAGRI AGLKVKRIIN EPTAAALAYG
     LDKGKGNKTI AVYDLGGGTF DISIIEIDDV DKEKTFEVLA TNGDTHLGGE DFDNRLINYL
     VEDFKKDQGT DLRNDSLAMQ RLKESAEKAK IELSSTQQTD VNLPYITADS TGPKHLNIKV
     TRSKLESLVE DLITRSIEPL KIALKDAKLS ISDIDDVILV GGQTRMPMVQ KKVAEFFKKE
     PRKDVNPDEA VAVGAAVQGG VLSGEVKDVL LLDVTPLSLG IETMGGVMTT LISKNTTIPT
     KHSQIFSTAE DNQTAVTIHV LQGERKRSID NKSLGQFNLD GIQPAPRGMA QIEVTFDIDS
     DGILHVSAKD KNTGKEQKIT IKASSGLNET EIKKMILDAE QNSESDQKFE ELVKVRNQGD
     QISHSTKKQL KDLEKTINVN DQKEINEALN KLDTALKGEN KTKIEEKIQE VLKISTKLIE
     KNKPKQTSES SNSNSPSSSK PEENVVDAEF EEVKDQKK