ID   DNAK_FRUSA              Reviewed;         614 AA.
AC   Q8KML6;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 73.
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};
OS   Fructilactobacillus sanfranciscensis (Lactobacillus sanfranciscensis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Fructilactobacillus.
OX   NCBI_TaxID=1625;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27651 / DSM 20451 / JCM 5668 / KCTC 3205 / NCIMB 702811 / NRRL
RC   B-3934 / L-12;
RA   Ehrmann M.A.;
RT   "Identification and characterization of the dnak operon of Lactobacillus
RT   sanfranciscensis.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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; AJ315382; CAC86402.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KML6; -.
DR   SMR; Q8KML6; -.
DR   PRIDE; Q8KML6; -.
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; 2.
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..614
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078477"
FT   REGION          576..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         176
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   614 AA;  66299 MW;  D0DDF2AA8875E711 CRC64;
     MASNKVIGID LGTTNSAVAV MEGGKPKIIT NPDGSRTTPS VVAFKNGEIQ VGEVAKRQEI
     TNPNTVRSIK SHMGEEGYTV DIDGKKYTPQ QISAMILQYI KGYAEDYLGD TVSEAVITVP
     AYFNDAQRQA TKDAGKIAGL DVKRIINEPT AAALAYGLDK QDKDEKILVY DLGGGTFDVS
     VLELGDGVFQ VLSTNGDTHL GGDDFDQRII DYLVAEFKKE NGVDLAQDKM ALQRLKDAAE
     KAKKELSGVN QTEISLPFIA SNDNGPLHLQ TTLTRAKFNE LTHDLVEKTK IPFENALKDA
     GLSTSDIDEV ILNGGSTRIP AVQEAVKEWS GKEPNHSINP DEAVALGAAV QGGVLTGDVK
     DVVLLDVTPL SLGIETMGGV MTKLIEKNTT IPTSKSQTFS TAADNQTAVD IHVLQGERPM
     AADNKSLGRF QLTDIPAAPR GIPQIEVTFD IDKNGIVNVS AKDKGTGKEQ KITIKDSNGL
     SDEEIEKMMN EAKANEEADK KKKEEVDLNN EVDQLIFQTD KTLKDVEGKV SEDEIKGVKD
     AEEELKKAKA DGNLDDMKAK KDTLNEKVQA VAVKLYQQQQ SQGGEAGAAN GDASKKDDNT
     VDGDFHEVHD DDKK