ID   DNAJ1_STRAL             Reviewed;          82 AA.
AC   P96457;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Chaperone protein DnaJ 1;
DE   Flags: Fragment;
GN   Name=dnaJ1;
OS   Streptomyces albus G.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=J1074;
RX   PubMed=9004222; DOI=10.1046/j.1365-2958.1997.1811563.x;
RA   Grandvalet C., Servant P., Mazodier P.;
RT   "Disruption of hspR, the repressor gene of the dnaK operon in Streptomyces
RT   albus G.";
RL   Mol. Microbiol. 23:77-84(1997).
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; U43299; AAB48077.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96457; -.
DR   SMR; P96457; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   SUPFAM; SSF49493; SSF49493; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; DNA replication; Metal-binding; Repeat;
KW   Stress response; Zinc.
FT   CHAIN           <1..82
FT                   /note="Chaperone protein DnaJ 1"
FT                   /id="PRO_0000070894"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   82 AA;  8663 MW;  BFE2CCF2845F5349 CRC64;
     YHLGGPPVTL KLPPGTPAGR TMRARGKGAV RKDGTRGDLL VTVDVAVPQH LSSEAREALE
     AYRKATADED PRAELFKAAK GA