ID   DNAK_BORRA              Reviewed;         632 AA.
AC   B5RPM1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=BRE_523;
OS   Borrelia recurrentis (strain A1).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=412418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1;
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}.
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DR   EMBL; CP000993; ACH94755.1; -; Genomic_DNA.
DR   RefSeq; WP_012538955.1; NC_011244.1.
DR   AlphaFoldDB; B5RPM1; -.
DR   SMR; B5RPM1; -.
DR   EnsemblBacteria; ACH94755; ACH94755; BRE_523.
DR   KEGG; bre:BRE_523; -.
DR   HOGENOM; CLU_005965_2_4_12; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000612; 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_1000119676"
FT   REGION          601..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;  68736 MW;  0F3766D4D97536E4 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 ENKIKELKDT LEGSDISLLK SKTEELQQAS YKIAEMMYKD
     AQASSPAQNN AQNNAGSESK EADYEVVDED KK