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 27-MAR-2024, entry version 142. 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 / DSM 19775 / NCTC 10195 / G37) OS (Mycoplasmoides genitalium). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; 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 / DSM 19775 / NCTC 10195 / G37; 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; Evidence={ECO:0000255|HAMAP- CC 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 AlphaFoldDB; P47265; -. DR SMR; P47265; -. DR STRING; 243273.MG_019; -. DR KEGG; mge:MG_019; -. DR eggNOG; COG0484; Bacteria. DR HOGENOM; CLU_017633_0_7_14; -. DR InParanoid; P47265; -. DR OrthoDB; 9779889at2; -. 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; cd10747; DnaJ_C; 1. DR CDD; cd10719; DnaJ_zf; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1. DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2. 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 NCBIfam; TIGR02349; DnaJ_bact; 1. DR PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1. DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 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; Chaperone J-domain; 1. DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1. DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2. 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 BINDING 164 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 167 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 182 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 208 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 211 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 222 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT BINDING 225 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="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 //