ID   DNAJ_SYNE7              Reviewed;         287 AA.
AC   P50026; Q31K10;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Chaperone protein DnaJ;
GN   Name=dnaJ; OrderedLocusNames=Synpcc7942_2579;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9240461; DOI=10.1006/bbrc.1997.6992;
RA   Oguchi K., Nimura K., Yoshikawa H., Takahashi H.;
RT   "Sequence and analysis of a dnaJ homologue gene in cyanobacterium
RT   Synechococcus sp. PCC7942.";
RL   Biochem. Biophys. Res. Commun. 236:461-466(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189.
RX   PubMed=8003021; DOI=10.1006/bbrc.1994.1778;
RA   Nimura K., Yoshikawa H., Takahashi H.;
RT   "Sequence analysis of the third dnaK homolog gene in Synechococcus sp.
RT   PCC7942.";
RL   Biochem. Biophys. Res. Commun. 201:848-854(1994).
RN   [4]
RP   ERRATUM OF PUBMED:8003021.
RX   PubMed=7811295; DOI=10.1006/bbrc.1994.2908;
RA   Nimura K., Yoshikawa H., Takahashi H.;
RL   Biochem. Biophys. Res. Commun. 205:2016-2017(1994).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB58609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB003519; BAA21679.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB58609.1; ALT_INIT; Genomic_DNA.
DR   EMBL; D29968; BAA06235.1; -; Genomic_DNA.
DR   PIR; JC5550; JC5550.
DR   PIR; PC2306; PC2306.
DR   AlphaFoldDB; P50026; -.
DR   SMR; P50026; -.
DR   STRING; 1140.Synpcc7942_2579; -.
DR   PRIDE; P50026; -.
DR   EnsemblBacteria; ABB58609; ABB58609; Synpcc7942_2579.
DR   KEGG; syf:Synpcc7942_2579; -.
DR   eggNOG; COG0484; Bacteria.
DR   HOGENOM; CLU_017633_0_0_3; -.
DR   BioCyc; SYNEL:SYNPCC7942_2579-MON; -.
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   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; DNA replication; Metal-binding; Repeat;
KW   Stress response; Zinc.
FT   CHAIN           1..287
FT                   /note="Chaperone protein DnaJ"
FT                   /id="PRO_0000070913"
FT   DOMAIN          6..71
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          108..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  31980 MW;  2927A269B2E6C546 CRC64;
     MQNFRDYYAL LGIPQSADQA AIKAAFRKLA RQCHPDLNPG DRQAEERFKQ ISEAYEILSD
     PDRRAEYQRF SRYWQQQGAA SVGSDDDYGD FPDFDIFVDE LLGRRTVERS PRRSARRSAA
     TSSALSRDLE RSLEVDPKTA LQGGSAQLQL EDGRLLEVDI PAGIQAGEYL RLRGQGIKGG
     DLLLRVQLQA SNFQVQGSDV IYTLNVSPAM AVLGGQVTVP TLDGPVQMKL PASLRSGQRL
     RLAGKGYSKP SGDRGDQIVV IQLQLPTRLS PEERQLYEQL RSLEQSR