ID   DNAK_BORBZ              Reviewed;         635 AA.
AC   B7J282; P28608;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=BbuZS7_0528;
OS   Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=445985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1356932; DOI=10.1128/iai.60.11.4856-4866.1992;
RA   Wallich R., Helmes C., Schaible U.E., Lobet Y., Moter S.E., Kramer M.D.,
RA   Simon M.M.;
RT   "Evaluation of genetic divergence among Borrelia burgdorferi isolates by
RT   use of OspA, fla, HSP60, and HSP70 gene probes.";
RL   Infect. Immun. 60:4856-4866(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS7;
RX   PubMed=20935092; DOI=10.1128/jb.01158-10;
RA   Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA   Mongodin E.F., Luft B.J.;
RT   "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL   J. Bacteriol. 193:1018-1020(2011).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR   EMBL; X67646; CAA47888.1; -; Genomic_DNA.
DR   EMBL; CP001205; ACK75037.1; -; Genomic_DNA.
DR   PIR; E70164; E70164.
DR   RefSeq; WP_002557108.1; NC_011728.1.
DR   AlphaFoldDB; B7J282; -.
DR   SMR; B7J282; -.
DR   PRIDE; B7J282; -.
DR   EnsemblBacteria; ACK75037; ACK75037; BbuZS7_0528.
DR   GeneID; 56567952; -.
DR   KEGG; bbz:BbuZS7_0528; -.
DR   HOGENOM; CLU_005965_2_4_12; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006901; 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   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN           1..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119672"
FT   REGION          597..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..635
FT                   /note="Basic and acidic 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   635 AA;  69276 MW;  D6F57BF413463B73 CRC64;
     MGKIIGIDLG TTNSCVAIME HGKPVVIQNS EGGRTTPSIV AYTNKGERLV GQVAKNQMVT
     NPENTIYSIK RFMGRRFEEV ASEIKMVPYK IEKGLNGDAR VNISNIKKQM SPPEISAATL
     TKMKETAEAY LGEKVTEAVI TVPAYFNDAQ RQATKDAGKI AGLEVKRIVN EPTAAALAYG
     IEKKHEEIVA VYDLGGGTFD ISILELGDGV FEVKSTNGDT HLGGDNFDDE IIKHLISEFK
     KESAIDLSND KMALQRLKEA AEKAKIELSG AQEASINLPF ITADANGPKH LQYTLTRAKF
     EQMVDHLVQK TKEPCLKAIK DAGLKASDIN EVILVGGSTR IPAIQKIVKD IFGQDPNKGV
     NPDEAVAIGA AIQGGILTGE TKDMVLLDVT PLSLGIETLG GVMTKLIERN TTIPTKKSQV
     FSTAADNQTS VDIKVLQGER EMAAQNRILG NFILDGIPAA PRGVPQIEVS FDIDANGIVH
     VSAKDMGTGK EQKIRIESSS GLSESEIDRM VKDAEAHAEE DKKLKENIEA KNTANSLIYQ
     TEKSLKEYSE KISSEDKEAI ESKIKELKES LEKEDISLIK SRTEELQKAS YKIAEMMYKD
     SSQQNANSQQ ENGPQSNTSE EGKEADYEVV DEDKK