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 26-FEB-2020, entry version 129. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; 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; DOI=10.1128/jb.175.24.7918-7930.1993; 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 sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71235.1; -; Genomic_DNA. DR EMBL; U01723; AAC43198.1; -; Genomic_DNA. DR PIR; A64202; A64202. DR RefSeq; WP_009885921.1; NZ_AAGX01000010.1. DR SMR; P47265; -. DR STRING; 243273.MG_019; -. DR EnsemblBacteria; AAC71235; AAC71235; MG_019. DR KEGG; mge:MG_019; -. DR eggNOG; ENOG4105BZ5; Bacteria. DR eggNOG; COG0484; LUCA. DR HOGENOM; CLU_017633_0_7_14; -. DR KO; K03686; -. DR OMA; MNMDDIF; -. DR OrthoDB; 1738789at2; -. DR BioCyc; MGEN243273:G1GJ2-19-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0042026; P:protein refolding; IBA:GO_Central. 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; Reference proteome; KW Repeat; Stress response; Zinc; Zinc-finger. FT CHAIN 1..389 FT /note="Chaperone protein DnaJ" FT /id="PRO_0000070824" FT DOMAIN 5..79 FT /note="J" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT REPEAT 164..171 FT /note="CXXCXGXG motif" FT REPEAT 182..189 FT /note="CXXCXGXG motif" FT REPEAT 208..215 FT /note="CXXCXGXG motif" FT REPEAT 222..229 FT /note="CXXCXGXG motif" FT ZN_FING 151..234 FT /note="CR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT COMPBIAS 84..134 FT /note="Gly-rich" FT METAL 164 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 167 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 182 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 185 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 208 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 211 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 222 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 225 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" 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 //