ID   DNAK_BIFLS              Reviewed;         631 AA.
AC   B7GT47; E8MND3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Blon_0141, BLIJ_0145;
OS   Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS   1222 / NCTC 11817 / S12).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=391904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA   Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA   Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA   Richardson P.M., Mills D.A.;
RT   "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT   adaptations for milk utilization within the infant microbiome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA   Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA   Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(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}.
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DR   EMBL; CP001095; ACJ51270.1; -; Genomic_DNA.
DR   EMBL; AP010889; BAJ67739.1; -; Genomic_DNA.
DR   RefSeq; WP_012576591.1; NZ_JDTT01000001.1.
DR   AlphaFoldDB; B7GT47; -.
DR   SMR; B7GT47; -.
DR   PRIDE; B7GT47; -.
DR   EnsemblBacteria; ACJ51270; ACJ51270; Blon_0141.
DR   KEGG; bln:Blon_0141; -.
DR   KEGG; blon:BLIJ_0145; -.
DR   PATRIC; fig|391904.8.peg.149; -.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   Proteomes; UP000001360; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:CAFA.
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:0002020; F:protease binding; IPI:CAFA.
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..631
FT                   /note="Chaperone protein DnaK"
FT                   /id="PRO_1000133133"
FT   REGION          586..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..631
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   631 AA;  67226 MW;  54C2DF24BBC5A32C CRC64;
     MARAVGIDLG TTNSCIATLE GGEPTVIVNA EGARTTPSVV AFSKSGEILV GEVAKRQAVT
     NVDRTISSVK RHMGTDWTVD IDGKKWTPQE ISAQILMKLK RDAEAYLGEP VTDAVITCPA
     YFNDAQRQAT KDAGKIAGLN VLRIINEPTA AALAYGLEKG KEDERILVFD LGGGTFDVSL
     LEIGKDDDGF STIQVQATNG DNHLGGDDWD QKIIDWLVSE VKNKYGVDLS KDKIALQRLK
     EAAEQAKKEL SSSTSTSISM QYLAMTPDGT PVHLDETLTR AHFEEMTSDL LGRCRTPFNN
     VLHDAGISVS DIDHVVLVGG STRMPAVKDL VKELTGGKEA NQSVNPDEVV AVGAAVQSGV
     IKGDRKDVLL IDVTPLSLGI ETKGGIMTKL IDRNTAIPTK RSEVFSTAED NQPSVLIQVY
     QGEREFARDN KPLGTFELTG IAPAPRGVPQ IEVTFDIDAN GIVHVSAKDK GTGKEQSMTI
     TGGSGLPKDE IDRMVKEAEA HEAEDKQRKE DAETRNQAEA FAYSTEKLVN DNKDKLSDDI
     VKEVTDKVNA LKEALKGDDT EKVKTAQTEL MTAAQKIGQV LYAQQGAEGA AAGAGAAGAA
     GAGASAGSAS GSDDDTVEAE VVDDDDDKDN K