DNAK_BIFLO
ID DNAK_BIFLO Reviewed; 626 AA.
AC Q8G6W1;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=BL0520;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24348.1; -; Genomic_DNA.
DR RefSeq; NP_695712.1; NC_004307.2.
DR RefSeq; WP_007051640.1; NC_004307.2.
DR AlphaFoldDB; Q8G6W1; -.
DR SMR; Q8G6W1; -.
DR STRING; 206672.BL0520; -.
DR MoonProt; Q8G6W1; -.
DR EnsemblBacteria; AAN24348; AAN24348; BL0520.
DR GeneID; 66504351; -.
DR KEGG; blo:BL0520; -.
DR PATRIC; fig|206672.9.peg.1259; -.
DR HOGENOM; CLU_005965_2_4_11; -.
DR OMA; ISIKRHM; -.
DR PhylomeDB; Q8G6W1; -.
DR Proteomes; UP000000439; 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_0000078423"
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