ID   DNAK_AQUPY              Reviewed;         605 AA.
AC   O86103;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
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;
DE   Flags: Fragment;
GN   Name=dnaK;
OS   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9882656; DOI=10.1128/jb.181.2.434-443.1999;
RA   Gribaldo S., Lumia V., Creti R., de Macario E.C., Sanangelantoni A.M.,
RA   Cammarano P.;
RT   "Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and
RT   sequence features of HSP70 suggest a novel outlook on phylogenies inferred
RT   from this protein.";
RL   J. Bacteriol. 181:434-443(1999).
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; AJ005800; CAA06703.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86103; -.
DR   SMR; O86103; -.
DR   PRIDE; O86103; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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; 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..>605
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078413"
FT   MOD_RES         202
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   NON_TER         605
SQ   SEQUENCE   605 AA;  67140 MW;  311AF03471AD477A CRC64;
     MAGKGKIIGI DLGNETNSVV AVMMGDEAVV IQNQEGSRLT PSVVSWTKEK EVLVGDPAKR
     RAILDPENTV YESKRFIGRK FEEVKEEAKR VSYKVVPDEK GDAAFDIPNA GKLVRPEEVG
     AHVLRKLKEA AEAFLGEPVK KAVITVPAYF NERQRQATKD AGKIAGLEVV RILNEPTRAA
     MAYGLHKKEN VRILVYDFGG GTFDVSILEG GDGVIEVKAT AGDTHLGGAN IDERIMEWLI
     EEFKKEHGID LRQDRTALQR LKEAAEQAKK ELSFKMETEI NLPFITIDPN TNQPLHLQKK
     LTRARLEEMI NDLIDRTIDI VKQALEDANV KPSDIDEVVL VGGSTRIPLV QQKIKEFFGK
     EPHKGLNPDE VVAMGAAIQA GVLAGEVKEI VLVDVTPLEL GVETYGGVMT VLIPRNTPIP
     VKKSKVFTTA HDYQTEVEIH VLHGERPLAK DNKSLAKFYL TGIPPAPRGV PKIEVCFDID
     ADGILHVTAK DLGTGKEQSV RVEISSGLTP EEIERIIKEA EETREEDRKK KELIEAKNQL
     DHLVYQLEKT LKEAGDKVPA DVKQEAEKVI EEAKKTIETA TDINEAKELQ KEFSRYPQSS
     EQPFT