ID   DNAK_BUCA5              Reviewed;         637 AA.
AC   B8D8V4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=BUAP5A_151;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=563178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5A;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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; CP001161; ACL30526.1; -; Genomic_DNA.
DR   RefSeq; WP_009874109.1; NC_011833.1.
DR   AlphaFoldDB; B8D8V4; -.
DR   SMR; B8D8V4; -.
DR   KEGG; bap:BUAP5A_151; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006904; 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_1000133135"
FT   REGION          599..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..637
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   637 AA;  70042 MW;  838C8C215A648BDE CRC64;
     MGKIIGIDLG TTNSCVAIMD GNKPRVLENA EGDRTTPSII AYTQEGEVLV GQPAKRQAIT
     NPKNTLFAIK RLIGRKFKDD EVQRDIKIMP YNIVNSDNGD AWIDVKKQKM APPQISAEVL
     KKMKKTAEDY LGETIKEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
     LDKGKGNRTI AVYDLGGGTF DISIIEIDEV DKEKTFEVLA TNGDTHLGGE DFDSRLINYL
     VTEFKKEQGI DLRNDPLSMQ RLKESAEKAK IELSSAQQTD VNLPYITADS NGPKHLNIKV
     TRAKLESLVE DLILRSIEPL KVALKDAGLS VTDINDVILV GGQTRMPMVQ SKVADFFGKE
     PRKDVNPDEA VAVGAAVQGG VLSGDVKDVL LLDVTPLSLG IETMGGIMTS LINKNTTIPT
     KHSQIFSTAE DNQSAVTIHV LQGERKRSSD NKSLGQFNLD GINPAPRGTA QIEVTFDIDS
     DGILHVSAKD KKTGKEQKIT IKASSGLNEE EIKKMVNDAE ANSEADQKFE ELIQTRNQGD
     QLVHSIKKQL NENKNSIEEE SKKDIQLALN KLENALKGED KSDIEKNIQN LLKISSKLTE
     INQKKSEKDQ KDNNMSANKK DENVVDAEFE EIKDPKK