ID   DNAK_LACPL              Reviewed;         622 AA.
AC   Q88VM0; F9UPY4;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=lp_2027;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL935263; CCC79273.1; -; Genomic_DNA.
DR   RefSeq; WP_011101636.1; NC_004567.2.
DR   RefSeq; YP_004889787.1; NC_004567.2.
DR   AlphaFoldDB; Q88VM0; -.
DR   SMR; Q88VM0; -.
DR   STRING; 220668.lp_2027; -.
DR   PRIDE; Q88VM0; -.
DR   EnsemblBacteria; CCC79273; CCC79273; lp_2027.
DR   KEGG; lpl:lp_2027; -.
DR   PATRIC; fig|220668.9.peg.1712; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OMA; ISIKRHM; -.
DR   PhylomeDB; Q88VM0; -.
DR   BioCyc; LPLA220668:G1GW0-1734-MON; -.
DR   Proteomes; UP000000432; 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; 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   Reference proteome; Stress response.
FT   CHAIN           1..622
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078475"
FT   REGION          527..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..622
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   622 AA;  66730 MW;  2E96385123969521 CRC64;
     MASNKIIGID LGTTNSAVAV LEGNEPKIIT TPEGGRTVPS VVAFKDGETQ VGEVAKRQAI
     TNPNTVASIK RHMGEAGYKV SIEGKDYTPQ QISAMILQYI KGFAEDYLGD TVEKAVVTVP
     AYFNDAQRQA TKDAGKIAGL NIERIINEPT AAALAYGLDK TDKDEKILVY DLGGGTFDVS
     ILELGDGVFE VLSTNGDTHL GGDDFDQKII DWLVDGFKAD NGVDLSKDKM ALQRLKDAAE
     KAKKDLSGVS EAQISLPFIS AGASGPLHLE TTLTRAKFNE LTADLVEKTR IPVENALKDA
     DLSASDLDVV ILNGGSTRIP AVQEAVEKWT GKESNHSINP DEAVALGAAV QGGVITGDVK
     DVVLLDVTPL SLGIETMGGV FTKLIDRNTT IPTSKSQVFS TAADNQPAVD IHVLQGERPM
     AADNKTLGRF QLTDIPAAPR GVPQIEVKFD IDKNGIVNVS AKDMGTNKEQ KITIKSSSGL
     SDDEIDQMVK EAKENEEADK KRKEEVDLKN EVDQLIFTTD KTLKDLEGKV SEDEVKKAKD
     ARDALKKAQD DNNIDEMKAK KDDLNKIVQD LSVKLYQQAQ EAQGAQGGAD SNAAGNANSA
     KGSDDNTVDG DFEDLDKDKD KK