ID   DNAK_BORHD              Reviewed;         632 AA.
AC   B2S0M0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=BH0518;
OS   Borrelia hermsii (strain HS1 / DAH).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 / DAH;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; CP000048; AAX17026.1; -; Genomic_DNA.
DR   RefSeq; WP_012422278.1; NC_010673.1.
DR   AlphaFoldDB; B2S0M0; -.
DR   SMR; B2S0M0; -.
DR   PRIDE; B2S0M0; -.
DR   KEGG; bhr:BH0518; -.
DR   HOGENOM; CLU_005965_2_4_12; -.
DR   OMA; ISIKRHM; -.
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_1000119674"
FT   REGION          600..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..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;  68716 MW;  86B1F000A06940B9 CRC64;
     MGKIIGIDLG TTNSCVAIME HGKPVVIQNS EGGRTTPSIV AYTNKGERLV GQVAKNQMVT
     NPENTIYSIK RFMGRRFEEV ASEIKMVPYK VEKGQNGDAR VNISNIKKQM SPPEISAATL
     TKMKETAEAY LGETVTEAVI TVPAYFNDAQ RQATKDAGKI AGLDVKRIVN EPTAAALAYG
     IEKKNEEIVA VYDLGGGTFD ISILELGDGV FEVKSTNGDT HLGGDNFDDE IIKHLITEFK
     KDSAIDLSND KMALQRLKEA AEKAKIELSS AQEASINLPF ITADANGPKH LQYTLTRAKF
     EQMVDHLVQK TKEPCLNAIK DAGLKASDIN EVILVGGSTR IPAIQKIVKE IFAQEPNKGV
     NPDEAVAIGA AIQGGILTGE TKDMVLLDVT PLSLGIETLG GVMTKLIERN TTIPTKKSQV
     FSTAADNQTS VDIKVLQGER EMASQNRVLG NFILDGIPAA PRGVPQIEVS FDIDANGIVH
     VSAKDMGTGK EQKIRIESSS GLSEEEIERM VRDAEAHAEE DKKLKESIET KNIANSLIYQ
     TEKSLKEYGD KITSEDKEAI ENKIKELKDA LEGSDVSSIK SKTEELQQAS YKIAEMMYKD
     AQASSSNQDN AQNNAGSESK EADYEVVDED KK