ID   DNAK_LEPBJ              Reviewed;         645 AA.
AC   Q04VC8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=LBJ_0433;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000350; ABJ75142.1; -; Genomic_DNA.
DR   RefSeq; WP_011670944.1; NC_008510.1.
DR   AlphaFoldDB; Q04VC8; -.
DR   SMR; Q04VC8; -.
DR   EnsemblBacteria; ABJ75142; ABJ75142; LBJ_0433.
DR   KEGG; lbj:LBJ_0433; -.
DR   HOGENOM; CLU_005965_2_4_12; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000656; Chromosome 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..645
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119721"
FT   REGION          602..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   645 AA;  69002 MW;  7A56721377421BB0 CRC64;
     MSKEKIIGID LGTTNSVVSV MEGGDPVVIQ NSEGARTTPS IVAFTAKGEN LVGQFAKNQA
     ITNAVNTIRS AKRFIGRRIG ECESEMKHVS YKVIRSGNEG VKFETSAGEF TPQEISARVL
     MKMKQTAEDY LGQKVTKAVI TVPAYFNDEQ RQATKDAGRI AGLEVERIIN EPTAAALAYG
     FDKKNVNSKI AVYDLGGGTF DISILELADG VFEVKSTNGD THLGGDDFDM AIMEWMISEF
     KNQTGIDISA DKNTVQRLKE AAEKAKIELS GTMSTQINLP FITADASGPK HLDMTLSRAK
     FDQLTKSLVD RTRIPCENAL RDAGLKASDI NEVILVGGSI RIPAVQELVK QIFGKEPNKS
     VNPDEVVAVG AAIQGGVLAG EVSDVLLLDV TPLSLGIETL GGVMTKLIER NTTIPTKKSQ
     VFSTAADNQS AVSIHVLQGE REMASANRTL GRFDLIGIPP APRGVPQIEV TFDIDANGIV
     HVSAKDLGTG KEQKIRIESS SGLSEDEIQK MVKDAEAHAA ADKAQREVIE AKNELDTLAY
     SLEKTVNEAG DKIGASEKQL ATDEVKRARE AIESNDKARM ESAKASISKI ASDIATKVYS
     QGAPGAEQAA GSTGPDQGQN DQGNSGNNGE KVVDADYTVV DDEKK