ID DNAJ_ACTPJ Reviewed; 380 AA. AC B0BTI6; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 25-MAY-2022, entry version 83. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=APJL_1952; OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=434271; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JL03; RX PubMed=18197260; DOI=10.1371/journal.pone.0001450; RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W., RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T., RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S., RA Zhao G.-P., Chen H.; RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of RT serotype 3 prevalent in China."; RL PLoS ONE 3:E1450-E1450(2008). 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; CC Evidence={ECO:0000255|HAMAP-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; CP000687; ABY70500.1; -; Genomic_DNA. DR RefSeq; WP_012263447.1; NC_010278.1. DR AlphaFoldDB; B0BTI6; -. DR SMR; B0BTI6; -. DR EnsemblBacteria; ABY70500; ABY70500; APJL_1952. DR KEGG; apj:APJL_1952; -. DR HOGENOM; CLU_017633_0_7_6; -. DR OMA; DLHCTVT; -. DR OrthoDB; 1738789at2; -. DR BioCyc; APLE434271:G1G8V-1984-MONOMER; -. DR Proteomes; UP000008547; 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; cd10719; DnaJ_zf; 1. DR Gene3D; 1.10.287.110; -; 1. 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 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; SSF46565; 1. DR SUPFAM; SSF49493; SSF49493; 2. DR SUPFAM; SSF57938; SSF57938; 1. DR TIGRFAMs; TIGR02349; DnaJ_bact; 1. 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..380 FT /note="Chaperone protein DnaJ" FT /id="PRO_1000137655" FT DOMAIN 5..70 FT /note="J" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT REPEAT 149..156 FT /note="CXXCXGXG motif" FT REPEAT 166..173 FT /note="CXXCXGXG motif" FT REPEAT 188..195 FT /note="CXXCXGXG motif" FT REPEAT 202..209 FT /note="CXXCXGXG motif" FT ZN_FING 136..214 FT /note="CR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 149 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 152 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 166 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 169 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 188 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 191 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 202 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 205 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" SQ SEQUENCE 380 AA; 40910 MW; 2B98D160B2831EA8 CRC64; MAKKDYYEVL GLQKGASEND IKRAYKRLAS KHHPDKNQGS KDAEEKFKEI NEAYEVLGDA EKRAAYDQYG HAAFEQGGGA GGFGGGFGGG GFGGFEDIFS EMFGGGFGSG GRRQRVVRGD DLRYDIEISL EEAVKGCKKD IRISTLAECD TCHGSGAEKG SKVETCSHCH GSGRIRRQQG FFVTEAVCPS CHGSGKKIEK PCKSCHGDGR VQKAKNLSVT IPAGVDTGNQ LRLSGEGAAG ENGAPAGDLY VVIHVREHDI FERDGSNLYC EVPISFTMAA LGGEIEVPTL DGKLKLKIPA ETQTGKLFRV RGKGVTSPRG GYAGDLICKV VVETPVALND EQKDLLRKLE ESLASKSKHR PQQEGFLDSV KNFFSNLGKH //