ID DNAJ_BUCAP Reviewed; 378 AA. AC Q8K9Y9; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN OrderedLocusNames=BUsg_145; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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 {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01152}; CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000255|HAMAP- CC Rule:MF_01152}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01152}. 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. CC {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE013218; AAM67713.1; -; Genomic_DNA. DR RefSeq; WP_011053680.1; NC_004061.1. DR AlphaFoldDB; Q8K9Y9; -. DR SMR; Q8K9Y9; -. DR STRING; 198804.BUsg_145; -. DR GeneID; 75258978; -. DR KEGG; bas:BUsg_145; -. DR eggNOG; COG0484; Bacteria. DR HOGENOM; CLU_017633_0_7_6; -. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro. DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR CDD; cd06257; DnaJ; 1. DR CDD; cd10747; DnaJ_C; 1. DR CDD; cd10719; DnaJ_zf; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1. DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2. DR HAMAP; MF_01152; DnaJ; 1. DR InterPro; IPR012724; DnaJ. 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; IPR001305; HSP_DnaJ_Cys-rich_dom. DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf. DR InterPro; IPR036869; J_dom_sf. DR NCBIfam; TIGR02349; DnaJ_bact; 1. DR PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1. DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR Pfam; PF00684; DnaJ_CXXCXGXG; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1. DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS51188; ZF_CR; 1. PE 3: Inferred from homology; KW Chaperone; Cytoplasm; DNA replication; Metal-binding; Repeat; KW Stress response; Zinc; Zinc-finger. FT CHAIN 1..378 FT /note="Chaperone protein DnaJ" FT /id="PRO_0000070746" FT DOMAIN 5..70 FT /note="J" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT REPEAT 146..153 FT /note="CXXCXGXG motif" FT REPEAT 163..170 FT /note="CXXCXGXG motif" FT REPEAT 185..192 FT /note="CXXCXGXG motif" FT REPEAT 199..206 FT /note="CXXCXGXG motif" FT ZN_FING 133..211 FT /note="CR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 149 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 166 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 188 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 199 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 202 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" SQ SEQUENCE 378 AA; 42469 MW; BB73F48DAF7A2D34 CRC64; MAKKDYYQIL GIPKSAEERE IKKAYKRLAM KYHPDRNQGD KNAENKFKEI KEAYEILINE EKRTAYDQYG HAAFENGYNQ NNTYSTFTSS TDFGDIFGDV FGDIFGGSRN QRVKKGADLC YNMEISLEEA VKGTTKEIRI PTFQKCKTCY GMGTSTGTKP NGCSTCHGKG QIHIRKGFFT VQQSCPTCNG IGTVIKNPCR MCRGQGRIKT NKTLSVKIPP GIDTNDKIRL SKEGEAGTNG AQPGDLYVQM KVNKHPIFER EENNLYCEVP INFTMAALGG EIEVPTLDGR VNLKIPSETQ SGKLFRIRGK GVKSVQSRSR GDLLCRVVVE TPVNLNEKQK YLLSELGNSF NGFRGDKNSP RSKRFFDGVK RFFDDLTK //