ID DNAJ_FRATU Reviewed; 371 AA. AC P48207; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 26-NOV-2014, entry version 79. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OS Francisella tularensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=263; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7590305; DOI=10.1016/0378-1119(95)00489-S; RA Zuber M., Hoover T.A., Dertzbaugh M.T., Court D.L.; RT "Analysis of the DnaK molecular chaperone system of Francisella RT tularensis."; RL Gene 164:149-152(1995). 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. 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 CC center 2 is essential for interaction with DnaK and for DnaJ CC activity. {ECO:0000255|HAMAP-Rule:MF_01152}. CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC -!- SIMILARITY: Contains 1 CR-type zinc finger. {ECO:0000255|HAMAP- CC Rule:MF_01152}. CC -!- SIMILARITY: Contains 1 J domain. {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; L43367; AAA69562.1; -; Genomic_DNA. DR ProteinModelPortal; P48207; -. DR SMR; P48207; 6-76. DR STRING; 177416.FTT_1268c; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. 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 Gene3D; 1.10.287.110; -; 1. DR Gene3D; 2.10.230.10; -; 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 Pfam; PF01556; CTDII; 1. DR Pfam; PF00226; DnaJ; 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; 3. 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 1 371 Chaperone protein DnaJ. FT /FTId=PRO_0000070786. FT DOMAIN 5 70 J. {ECO:0000255|HAMAP-Rule:MF_01152}. FT REPEAT 140 147 CXXCXGXG motif. FT REPEAT 156 163 CXXCXGXG motif. FT REPEAT 178 185 CXXCXGXG motif. FT REPEAT 192 199 CXXCXGXG motif. FT ZN_FING 127 204 CR-type. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT COMPBIAS 79 110 Gly-rich. FT METAL 140 140 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 143 143 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 156 156 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 159 159 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 178 178 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 181 181 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 192 192 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. FT METAL 195 195 Zinc 1. {ECO:0000255|HAMAP- FT Rule:MF_01152}. SQ SEQUENCE 371 AA; 41481 MW; BBDC7F3B4741EF1E CRC64; MQQKCYYEIL NISKTASGVE IKRAYRKLAM KYHPDRNPGD KEAEIKFKEI SEAYEILSDD SKRSRYDQFG HAGVNQQSGF GGTGGFEDIF DTFFGGGTSR GSNRSRASRG SDLEYTLEIT LEEAFFGVEK EITIPRMESC DSCDGTGSKS RSKTTCHACH GQGTIRRQQG FFAFEQTCPV CNGTGYSITD PCDACYGNGK VKKQKTLKVK IPEGVDNGDR IRLQGEGDSG SNGAMNGDLY VQIIIKEHKI FERRDINLYC EMPISFTKAC LGGDIKVPTL DGEVVLKVVP ETQTGKVFRL REKGMKSLRG HRRGDLLCKV VVETPVNLSA EQKELLEKFA DSLGEDYQSK HAPKSKTWFD NVKDYAKKFF E //