ID   DNAK_LEPBA              Reviewed;         644 AA.
AC   B0SHT1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=LBF_3265;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / Ames;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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; CP000777; ABZ95732.1; -; Genomic_DNA.
DR   RefSeq; WP_012390299.1; NC_010842.1.
DR   AlphaFoldDB; B0SHT1; -.
DR   SMR; B0SHT1; -.
DR   KEGG; lbf:LBF_3265; -.
DR   HOGENOM; CLU_005965_2_4_12; -.
DR   OMA; ISIKRHM; -.
DR   BioCyc; LBIF355278:LBF_RS16590-MON; -.
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..644
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119720"
FT   REGION          550..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..583
FT                   /note="Basic and acidic 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   644 AA;  69046 MW;  D1989559E2D0B132 CRC64;
     MSKEKIIGID LGTTNSCVAV MEGGDPVVIQ NSEGARTTPS IVAFTAKGET IVGQFAKNQA
     ITNAVNTIRS AKRFIGRRFN EAGDESKMVS YKVIRAGNDG VKFETVSGEF TPQEIAARVL
     QKMKKTAEDF LGHEVKKAVV TVPAYFNDEQ RQATKDAGRI AGLEVERIIN EPTAAALAYG
     FDKKKTNAKI AVYDLGGGTF DVSILELGDG VFEVKSTNGD THLGGDDFDN VVMQWMIDEF
     KKQTGIDISG DKNTVQRLKE AAEKAKIELS GTSSTQINLP FITADASGPK HLDMTLTKAK
     FDEITRSLVE RTRIPCINAL KDAGLSASEI DEVILVGGSI RIPAVQALVK EIFGKEPNKS
     VNPDEVVAVG AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVMTKLIER NTTIPTRKSQ
     VFSTAADNQT TVSVHVLQGE REMASANRTL GRFDLVGIPS APRGVPQIEV TFDIDANGIV
     HVSAKDLGTG KEQKIRIESS SGLSEEEIKK MVKDAEAHAE EDKKLREAAD TKNELEAIVY
     QLEKTIGESA DKLDESEKQR AQDEIKRGRE AMESGDLERM KASRDSIQQV AMQIGQKIYS
     QAGPEQGAPG AEAGAGASQG ASGTDANGEK VVDADYTVVD EDKK