ID   DNAK_BORAP              Reviewed;         635 AA.
AC   Q0SMZ0; G0IQ71;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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};
GN   OrderedLocusNames=BAPKO_0545, BafPKo_0533;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01788.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69741.1; -; Genomic_DNA.
DR   RefSeq; WP_004789842.1; NC_017238.1.
DR   AlphaFoldDB; Q0SMZ0; -.
DR   SMR; Q0SMZ0; -.
DR   STRING; 390236.BafPKo_0533; -.
DR   EnsemblBacteria; AEL69741; AEL69741; BafPKo_0533.
DR   KEGG; baf:BAPKO_0545; -.
DR   KEGG; bafz:BafPKo_0533; -.
DR   PATRIC; fig|390236.22.peg.514; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_12; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000005216; 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..635
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059516"
FT   REGION          599..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..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;  69362 MW;  7557326E7E969475 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 KISIEDKETI ENKIKELKES LEKEDISLIK SKTEELQKAS YKIAEMMYKD
     SSQQNASNQQ ENGTQNNTSE EGKEADYEVV DEDKK