ID   DNAK_BIFAA              Reviewed;         626 AA.
AC   A1A3P5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=BAD_1547;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) 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; AP009256; BAF40328.1; -; Genomic_DNA.
DR   RefSeq; WP_011743845.1; NC_008618.1.
DR   AlphaFoldDB; A1A3P5; -.
DR   SMR; A1A3P5; -.
DR   STRING; 1680.BADO_1461; -.
DR   PRIDE; A1A3P5; -.
DR   EnsemblBacteria; BAF40328; BAF40328; BAD_1547.
DR   KEGG; bad:BAD_1547; -.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000008702; 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   Reference proteome; Stress response.
FT   CHAIN           1..626
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000059514"
FT   REGION          469..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..516
FT                   /note="Basic and 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;  66840 MW;  D9C4B8B23524904A CRC64;
     MGRAVGIDLG TTNSCIATLE GGQPTVIVNA EGARTTPSVV AFSKSGEILV GEVAKRQAVT
     NVDRTISSVK RHMGTDWTVE IDGKKWTPQE ISAQVLMKLK RDAEAYLGEP VTDAVITCPA
     YFNDAQRQAT KDAGTIAGLN VLRIINEPTA AALAYGLEKG KEDERILVFD LGGGTFDVSL
     LEIGKDDDGF STIQVQATNG DNHLGGDDWD QKIIDWLVGE VKNKYGVDLS KDKIALQRLK
     EAAEQAKKEL SSSTSTSISM QYLAMTPDGT PVHLDETLTR AHFEEMTSDL LGRCRTPFNN
     VLRDAGIGVS DIDHVVLVGG STRMPAVKEL VKELTGGKEA NQSVNPDEVV AVGAAVQSGV
     IKGDRKDVLL IDVTPLSLGI ETKGGIMTKL IERNTAIPTK RSEVFSTAED NQPSVLIQVY
     QGEREFARDN KPLGTFELTG IAPAPRGVPQ IEVTFDIDAN GIVHVSAKDK GTGKEQSMTI
     TGGSGLPKDE IDRMVKEAEA HEAEDKKRKE DAETRNQAES FAYQTEKLVN DNKDKLSDDV
     AKEVTDKVNE LKEALKGEDI EKIKSAQTEL MTSAQKIGQA LYAQQGAADA AGAAGAAGAG
     AAGSASNGSD DDVVDAEVVD DDKDNK