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 19-OCT-2011, entry version 35. DE RecName: Full=Chaperone protein DnaJ; GN Name=dnaJ; 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., RA Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., RA Zhang L., Xu T., Zheng H., Pu S., Wang B., Gu W., Zhang X.L., RA Zhu G.-F., Wang S., 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 CC and heat shock by preventing the aggregation of stress-denatured CC proteins and by disaggregating proteins, also in an autonomous, CC DnaK-independent fashion. Unfolded proteins bind initially to CC DnaJ; upon interaction with the DnaJ-bound protein, DnaK CC hydrolyzes its bound ATP, resulting in the formation of a stable CC complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers CC the release of the substrate protein, thus completing the reaction CC cycle. Several rounds of ATP-dependent interactions between DnaJ, CC DnaK and GrpE are required for fully efficient folding. Also CC involved, together with DnaK and GrpE, in the DNA replication of CC plasmids through activation of initiation proteins (By CC similarity). CC -!- COFACTOR: Binds 2 zinc ions per monomer (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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 CC center 2 is essential for interaction with DnaK and for DnaJ CC activity (By similarity). CC -!- SIMILARITY: Belongs to the DnaJ family. CC -!- SIMILARITY: Contains 1 CR-type zinc finger. CC -!- SIMILARITY: Contains 1 J domain. 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; YP_001652944.1; NC_010278.1. DR ProteinModelPortal; B0BTI6; -. DR SMR; B0BTI6; 2-78. DR STRING; B0BTI6; -. DR GeneID; 5852738; -. DR GenomeReviews; CP000687_GR; APJL_1952. DR KEGG; apj:APJL_1952; -. DR HOGENOM; HBG635315; -. DR OMA; EAEEHFK; -. DR ProtClustDB; PRK10767; -. DR BioCyc; APLE434271:APJL_1952-MONOMER; -. 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: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 GO; GO:0009408; P:response to heat; IEA:InterPro. DR HAMAP; MF_01152; DnaJ; 1; -. DR InterPro; IPR012724; DnaJ. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001623; DnaJ_N. DR InterPro; IPR018253; Heat_shock_DnaJ_CS. DR InterPro; IPR008971; HSP40/DnaJ_pept-bd. DR InterPro; IPR003095; Hsp_DnaJ. DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom. DR Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1. DR Gene3D; G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 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; DnaJ_N; 1. DR SUPFAM; SSF49493; HSP40_DnaJ_pep; 2. DR SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 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; Complete proteome; Cytoplasm; DNA replication; KW Metal-binding; Repeat; Stress response; Zinc; Zinc-finger. FT CHAIN 1 380 Chaperone protein DnaJ. FT /FTId=PRO_1000137655. FT DOMAIN 5 70 J. FT REPEAT 149 156 CXXCXGXG motif. FT REPEAT 166 173 CXXCXGXG motif. FT REPEAT 188 195 CXXCXGXG motif. FT REPEAT 202 209 CXXCXGXG motif. FT ZN_FING 136 214 CR-type. FT COMPBIAS 77 119 Gly-rich. FT METAL 149 149 Zinc 1 (By similarity). FT METAL 152 152 Zinc 1 (By similarity). FT METAL 166 166 Zinc 2 (By similarity). FT METAL 169 169 Zinc 2 (By similarity). FT METAL 188 188 Zinc 2 (By similarity). FT METAL 191 191 Zinc 2 (By similarity). FT METAL 202 202 Zinc 1 (By similarity). FT METAL 205 205 Zinc 1 (By similarity). 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 //