ID   DNAK_BIFLD              Reviewed;         626 AA.
AC   B3DNP9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=BLD_1313;
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=205913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A;
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(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; CP000605; ACD98758.1; -; Genomic_DNA.
DR   RefSeq; WP_007051640.1; NZ_AABM02000012.1.
DR   AlphaFoldDB; B3DNP9; -.
DR   SMR; B3DNP9; -.
DR   PRIDE; B3DNP9; -.
DR   EnsemblBacteria; ACD98758; ACD98758; BLD_1313.
DR   GeneID; 66504351; -.
DR   KEGG; blj:BLD_1313; -.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000002419; 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; 2.
DR   Pfam; PF00012; HSP70; 2.
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..626
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000119671"
FT   REGION          586..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..626
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   626 AA;  66943 MW;  099FC925DF8406E2 CRC64;
     MARAVGIDLG TTNSCIATLE GGEPTVIVNA EGARTTPSVV AFSKSGEILV GEVAKRQAVT
     NVDRTISSVK RHMGSDWTVD IDGKKWTPQE ISAQILMKLK RDAEAYLGEP VTDAVITCPA
     YFNDAQRQAT KDAGKIAGLN VLRIINEPTA AALAYGLEKG KEDERILVFD LGGGTFDVSL
     LEIGKDDDGF STIQVQATNG DNHLGGDDWD QKIIDWLVSE VKNKYGVDLS KDKIALQRLK
     EAAEQAKKEL SSSTSTSISM QYLAMTPDGT PVHLDETLTR AHFEEMTSDL LGRCRTPFNN
     VLHDAGISVS DIDHVVLVGG STRMPAVKEL VKELTGGKEA NQSVNPDEVV AVGAAVQSGV
     IKGDRKDVLL IDVTPLSLGI ETKGGIMTKL IDRNTAIPTK RSEVFSTAED NQPSVLIQVY
     QGEREFARDN KPLGTFELTG IAPAPRGVPQ IEVTFDIDAN GIVHVSAKDK GTGKEQSMTI
     TGGSGLPKDE IDRMVKEAEA HEAEDKKRKE DAETRNQAEA FAYSTEKLVN DNKDKLSDDI
     VKEVTDKVNA LKEALKGDDT EKVKTAQTEL MTAAQKIGQV LYAQQGAEGA AAGADGAGAS
     AGSASGSDDD TVEAEVVDDD DDKDNK