ID   DNAK_AGGAC              Reviewed;         633 AA.
AC   P71331;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK;
OS   Aggregatibacter actinomycetemcomitans (Actinobacillus
OS   actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43718 / FDC Y4 / Serotype b;
RA   Yoshida A., Nakano Y., Yamashita Y., Yu H., Ohishi M., Koga T.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; D87753; BAA13454.1; -; Genomic_DNA.
DR   AlphaFoldDB; P71331; -.
DR   SMR; P71331; -.
DR   STRING; 714.ACT75_02525; -.
DR   PRIDE; P71331; -.
DR   eggNOG; COG0443; Bacteria.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..633
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078404"
FT   REGION          598..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   633 AA;  68394 MW;  5A2D630DD6822933 CRC64;
     MGKIVGIDLG TTNSCVAVME GEKPRVIENA EGDRTTPSII AYTNDNETLV GQPAKRQAVT
     NPKNTLFAIK RLIGRRFEDE EVKRDIDIMP FAITKADNGD AWVEVKGEKL APPQISAEVL
     KKMKKAAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
     LDKGTGNKTI AVYDLGGGTF DLSIIEIDEV GGEKTFEVLA TNGDTHLGGE DFDNRIINYL
     VDEFKKEQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHLNIKL
     TRAKLESLVE DLVAKSLEPV RIALKDAGKS PSEIDDVILV GGQTRMPLVQ QEVEKFFGKA
     PRKDVNPDEA VAIGAAVQGG VLAGDVKDVL LLDVTPLSLG IETMGGVMTT LIEKNTTIPT
     KKSQVFSTAE DNQSAVTIHV LQGERKQASA NKSLGQFNLE GINPVPRGMP QIEVTFDIDA
     DGIIHVSAKD KGTGKEQQIT IKSSSGLSDE EIQQMVRDAE ANAESDRKFE ELVQARNQAD
     HLIHSTRKQL DEAGDKVPAA DRGTIESALS DLEKAAKGED KAVIEAKIKA LAEVAQKLAQ
     TAQPHGDPQQ AQSNSKPNDD VVDAEFEEVK DNK