ID   DNAK_HAMD5              Reviewed;         635 AA.
AC   C4K3I6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=HDEF_0372;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(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; CP001277; ACQ67129.1; -; Genomic_DNA.
DR   RefSeq; WP_012738089.1; NC_012751.1.
DR   AlphaFoldDB; C4K3I6; -.
DR   SMR; C4K3I6; -.
DR   STRING; 572265.HDEF_0372; -.
DR   PRIDE; C4K3I6; -.
DR   EnsemblBacteria; ACQ67129; ACQ67129; HDEF_0372.
DR   GeneID; 66260282; -.
DR   KEGG; hde:HDEF_0372; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002334; 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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000205191"
FT   REGION          598..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..635
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   635 AA;  68927 MW;  A95638B027842528 CRC64;
     MTKIIGIDLG TTNSCVAIMD GSKPRVLENS EGDRTTPSII AYTDDGETLV GQPAKRQAVT
     NAKNTFFAIK RLVGRKFSDQ ETQRDKDIMP FDILESDNGD AWLSVKGQKT APPQISAEVL
     KKMKKTAEDY LGETVTEAVV TVPAYFNDAQ RQATKDAGRI SGLEIKRIIN EPTAAAIAYG
     LDKGKGNSTI AVYDLGGGTF DISIIEIDDV DGEKTFEVLA TNGDTHLGGE DFDNRLINYL
     VDEFKKEQGF DLRKDPLAMQ RLKEAAEKAK VELSSAQQTD VNLPYITADA TGPKHMNMKV
     TRAKLESLVE DLVSRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVADFFGKE
     PRKDVNPDEA VAIGAAVQGG VLSGEVKDLL LLDVTPLSLG IETMGGVMTS LISKNTTIPT
     KHSQVFSTAE DNQSAVTIHV LQGERKRAID NKSLGQFNLD GIQPAPRGTS QIEVTFDIDA
     DGILHVSAKD KNTGREQKIT IKASSGLSEA EIEKMVRDAE SNSETDRKFE ELIQVRNQAD
     HLIHATNKKL KEAGDKVSPE EKTSIEQALK ALETAIKGED KTDIESKANA LTMVSAKLEE
     ASQQNSSSNN AEKNDSSDVK ADAVDAEFEE VKDKK