ID   DNAK_NAEFO              Reviewed;          20 AA.
AC   P83724;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Chaperone protein dnaK;
DE   AltName: Full=NF024;
DE   Flags: Fragment;
OS   Naegleria fowleri (Brain eating amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5763 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 30214 / Nf 66;
RA   Omura M., Furushima-Shimogawara R., Izumiyama S., Endo T.;
RT   "Comparative study of protein profiles on pathogenic and nonpathogenic
RT   Naegleria species by 2D-PAGE.";
RL   Submitted (DEC-2003) to UniProtKB.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250|UniProtKB:O06430}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250|UniProtKB:O06430}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.7,
CC       its MW is: 46 kDa. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing; Nucleotide-binding;
KW   Phosphoprotein; Stress response.
FT   CHAIN           1..>20
FT                   /note="Chaperone protein dnaK"
FT                   /id="PRO_0000078308"
FT   NON_TER         20
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   20 AA;  2074 MW;  B583F8044B18EAD4 CRC64;
     KIIGIDLGTT NSXVAVMESN