ID   DNAK_LEPIC              Reviewed;         646 AA.
AC   P61442; O51869; P71442;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Chaperone protein DnaK;
DE   AltName: Full=HSP70;
DE   AltName: Full=Heat shock 70 kDa protein;
DE   AltName: Full=Heat shock protein 70;
GN   Name=dnaK; OrderedLocusNames=LIC_10524;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Wijnberg;
RX   PubMed=9714717; DOI=10.1016/s0378-1119(98)00329-1;
RA   Ballard S.A., Go M., Segers R.P.A.M., Adler B.;
RT   "Molecular analysis of the dnaK locus of Leptospira interrogans serovar
RT   Copenhageni.";
RL   Gene 216:21-29(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AF007813; AAC35416.1; -; Genomic_DNA.
DR   EMBL; AE016823; AAS69145.1; -; Genomic_DNA.
DR   RefSeq; WP_000031821.1; NC_005823.1.
DR   AlphaFoldDB; P61442; -.
DR   SMR; P61442; -.
DR   PaxDb; P61442; -.
DR   EnsemblBacteria; AAS69145; AAS69145; LIC_10524.
DR   GeneID; 61143879; -.
DR   KEGG; lic:LIC_10524; -.
DR   HOGENOM; CLU_005965_2_1_12; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000007037; Chromosome I.
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..646
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_0000078480"
FT   REGION          598..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         199
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        617
FT                   /note="Missing (in Ref. 1; AAC35416)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   646 AA;  69099 MW;  8C63B784AA32AB97 CRC64;
     MSKEKIIGID LGTTNSVVSV MEGGDPVVIQ NSEGARTTPS IVAFTAKGET LIGQFAKNQA
     ITNAVNTIRS AKRFIGRRLN ECESEMKHVS YKVIRSGNEG VKFETSAGEF TPQEISARVL
     MKMKQTAEDY LGQKVTKAVI TVPAYFNDEQ RQATKDAGRI AGLEVERIIN EPTAAALAYG
     FDKKNVNSKI AVYDLGGGTF DISILELADG VFEVKSTNGD THLGGDDFDM AIMEWMISEF
     KNQTGIDISA DKNTVQRLKE AAEKAKIELS GTMSTQINLP FITADASGPK HLDMTLTRAK
     FDQLTKSLVD RTRIPCENAL RDAGLKASDI NEVILVGGSI RIPAVQELVK QVFGKEPNKS
     VNPDEVVAIG AAIQGGVLAG EVSDVLLLDV TPLSLGIETL GGVMTKLIER NTTIPTKKSQ
     VFSTAADNQS AVSIHVLQGE REMASANRTL GRFDLIGIPP APRGVPQIEV TFDIDANGIV
     HVSAKDLGTG KEQKIRIESS SGLSEDEIQK MVKDAEAHAA ADKAQREVIE AKNELDTLTY
     SLEKTVNEAG DKIGANEKQL ATDEIKRARE AIESNDKARI ESAKASISKI ATDIASKVYS
     QSAPGAEQAA AGGPNGGAGS NDQGNSTNNG EKVVDADYTV VDDEKK