ID   DNAK_BORDL              Reviewed;         632 AA.
AC   B5RM75;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=BDU_520;
OS   Borrelia duttonii (strain Ly).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=412419;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ly;
RX   PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA   Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA   Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT   "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT   relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL   PLoS Genet. 4:E1000185-E1000185(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}.
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; CP000976; ACH93461.1; -; Genomic_DNA.
DR   RefSeq; WP_012538270.1; NC_011229.1.
DR   AlphaFoldDB; B5RM75; -.
DR   SMR; B5RM75; -.
DR   STRING; 412419.BDU_520; -.
DR   PRIDE; B5RM75; -.
DR   EnsemblBacteria; ACH93461; ACH93461; BDU_520.
DR   KEGG; bdu:BDU_520; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_12; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000000611; 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   Stress response.
FT   CHAIN           1..632
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119673"
FT   REGION          598..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   632 AA;  68750 MW;  0F2E5AF1D97523F1 CRC64;
     MGKIIGIDLG TTNSCVAIME HGKPVVIQNS EGGRTTPSIV AYTNKGERLV GQVAKNQMVT
     NPENTIYSIK RFMGRRFEEV ASEIKMVPYK VEKGQNGDAR VNISNIKKQM SPPEISAATL
     TKMKETAEAY LGEKVTEAVI TVPAYFNDAQ RQATKDAGKI AGLDVKRIVN EPTAAALAYG
     IEKKHEEIVA VYDLGGGTFD ISILELGDGV FEVKSTNGDT HLGGDNFDDE IIKYLITEFK
     KDSAIDLSND KMALQRLKEA AEKAKIELSG AQEASINLPF ITADANGPKH LQYTLTRAKF
     EQMVDHLVQK TKEPCLKAIK DAGLKASDIN EVILVGGSTR IPAIQKIVKE IFGQEPNKGV
     NPDEAVAIGA AIQGGILTGE AKDMVLLDVT PLSLGIETLG GVMTKLIERN TTIPTKKSQV
     FSTAADNQTS VDIKVLQGER EMASQNRVLG NFILDGIPAA PRGVPQIEVS FDIDANGIVH
     VSAKDMGTGK EQKIRIESSS GLSEEEIERM VKDAESHAEE DKKLKEGIEA KNIANSLIYQ
     TEKSLKEYGE KITNQDKEAI ENKIKELKDA LEGSDISLLK SKTEELQQAS YKIAEMMYKD
     AQASSPDQNN AQNNAGSESK EADYEVVDED KK