ID   DNAJ2_SYNY3             Reviewed;         307 AA.
AC   P73097;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Chaperone protein DnaJ 2;
GN   Name=dnaJ2; OrderedLocusNames=sll1933;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17122.1; -; Genomic_DNA.
DR   PIR; S75208; S75208.
DR   AlphaFoldDB; P73097; -.
DR   SMR; P73097; -.
DR   IntAct; P73097; 3.
DR   STRING; 1148.1652198; -.
DR   PaxDb; P73097; -.
DR   EnsemblBacteria; BAA17122; BAA17122; BAA17122.
DR   KEGG; syn:sll1933; -.
DR   eggNOG; COG0484; Bacteria.
DR   InParanoid; P73097; -.
DR   OMA; NPDGCTM; -.
DR   PhylomeDB; P73097; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
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; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; DNA replication; Reference proteome; Repeat;
KW   Stress response.
FT   CHAIN           1..307
FT                   /note="Chaperone protein DnaJ 2"
FT                   /id="PRO_0000070916"
FT   DOMAIN          6..71
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          69..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   307 AA;  34698 MW;  1BF6525D723223EF CRC64;
     MEQVRNYYQI LGVPRNATAE EIKKSFRKLA RQYHPDVNPN DKTAEEKFKD INEAYDVLSD
     ETKRRELDSR LFGRFRRPPT SRFSPNSNGG RSPNGTSVNG QVRTPTGRTG TRQPAQSWQD
     FSETRRTKVV SPARPVPRDV EANLTLPLEK AYRGGKERIR LEDGRSLEVE MPGGMGDGQR
     IRLKQQGING GDLYLKINLS PHPLFTLQGT DIACQVPVTP SEAILGGAIE VMTIDGLVKM
     TVPAGLKNGQ KLRLAKKGFP NNQGDRGDQL VEIRVEIPPE PSPEELELYR RIREKETFNP
     RQKFFDF