ID DNAJ_MYCGE Reviewed; 389 AA. AC P47265; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 03-SEP-2014, entry version 99. DE RecName: Full=Chaperone protein DnaJ; GN Name=dnaJ; OrderedLocusNames=MG019; OS Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195). OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15. RC STRAIN=ATCC 33530 / G-37 / NCTC 10195; RX PubMed=8253680; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random RT sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71235.1; -; Genomic_DNA. DR EMBL; U01723; AAC43198.1; -; Genomic_DNA. DR PIR; A64202; A64202. DR RefSeq; NP_072679.1; NC_000908.2. DR RefSeq; WP_009885921.1; NZ_AAGX01000010.1. DR ProteinModelPortal; P47265; -. DR STRING; 243273.MG_019; -. DR EnsemblBacteria; AAC71235; AAC71235; MG_019. DR GeneID; 875219; -. DR KEGG; mge:MG_019; -. DR PATRIC; 20009414; VBIMycGen98045_0017. DR eggNOG; COG0484; -. DR KO; K03686; -. DR OMA; HEKFTRK; -. DR OrthoDB; EOG6BPDKP; -. DR BioCyc; MGEN243273:GH2R-19-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; Complete proteome; Cytoplasm; DNA replication; KW Metal-binding; Repeat; Stress response; Zinc; Zinc-finger. FT CHAIN 1 389 Chaperone protein DnaJ. FT /FTId=PRO_0000070824. FT DOMAIN 5 79 J. FT REPEAT 164 171 CXXCXGXG motif. FT REPEAT 182 189 CXXCXGXG motif. FT REPEAT 208 215 CXXCXGXG motif. FT REPEAT 222 229 CXXCXGXG motif. FT ZN_FING 151 234 CR-type. FT COMPBIAS 84 134 Gly-rich. FT METAL 164 164 Zinc 1 (By similarity). FT METAL 167 167 Zinc 1 (By similarity). FT METAL 182 182 Zinc 2 (By similarity). FT METAL 185 185 Zinc 2 (By similarity). FT METAL 208 208 Zinc 2 (By similarity). FT METAL 211 211 Zinc 2 (By similarity). FT METAL 222 222 Zinc 1 (By similarity). FT METAL 225 225 Zinc 1 (By similarity). SQ SEQUENCE 389 AA; 43746 MW; 10614543F4B6ACDE CRC64; MAAGKRDYYE VLGISKNASS QDIKRAFRKL AMQYHPDRHK AENETTQKQN EEKFKEVNEA YEVLSDEEKR KLYDQFGHEG LNASGFHEAG FNPFDIFNSV FGEGFSFGMD GDSPFDFIFN RSKKRQQQIV VPYNLDIALV IEINFFEMTN GCNKTIKYER KVSCHSCNGF GAEGGESGLD LCKDCNGNGF VIKNQRSIFG TIQSQVLCST CNGQGKQIKV KCKTCRSNKY TVTNQIKEIN IPAGMYSGEA LVDESGGNEF KGHYGKLIIQ VNVLASKIFK RSDNNVIANV LVDPMVAIVG GVIELPTLEG IKEFNIRPGT KSGEQIVIPN GGIKFSKSFK RKAGDLIIII SYARPCEYTN LELKKLREFI KPNQEVKQYL NTLKNEYKT //