DNAJ_STRAG
ID DNAJ_STRAG Reviewed; 24 AA.
AC P95694;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Chaperone protein DnaJ;
DE Flags: Fragment;
GN Name=dnaJ;
OS Streptococcus agalactiae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1311;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rioux C.R., Martin D., Hamel J., Brodeur B.R.;
RT "Heat shock protein HSP70 and amino terminus of DnaJ of Streptococcus
RT agalactiae.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates actively in the response to hyperosmotic and
CC heat shock by preventing the aggregation of stress-denatured proteins
CC and by disaggregating proteins, also in an autonomous, DnaK-independent
CC fashion. Unfolded proteins bind initially to DnaJ; upon interaction
CC with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting
CC in the formation of a stable complex. GrpE releases ADP from DnaK; ATP
CC binding to DnaK triggers the release of the substrate protein, thus
CC completing the reaction cycle. Several rounds of ATP-dependent
CC interactions between DnaJ, DnaK and GrpE are required for fully
CC efficient folding. Also involved, together with DnaK and GrpE, in the
CC DNA replication of plasmids through activation of initiation proteins
CC (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK
CC ATPase activity. Zinc center 1 plays an important role in the
CC autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2
CC is essential for interaction with DnaK and for DnaJ activity (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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DR EMBL; U72719; AAB39220.1; -; Genomic_DNA.
DR AlphaFoldDB; P95694; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR036869; J_dom_sf.
DR SUPFAM; SSF46565; SSF46565; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; DNA replication; Metal-binding; Repeat;
KW Stress response; Zinc.
FT CHAIN 1..>24
FT /note="Chaperone protein DnaJ"
FT /id="PRO_0000070893"
FT DOMAIN 3..>24
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT NON_TER 24
SQ SEQUENCE 24 AA; 2760 MW; 342AE656E00913FC CRC64;
MNNTEFYDRL GVSKDASQDE IKKA