ID A0A7W4V0A5_9MICO Unreviewed; 372 AA. AC A0A7W4V0A5; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 27-NOV-2024, entry version 14. DE RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152}; GN ORFNames=FHX49_000059 {ECO:0000313|EMBL:MBB2974518.1}; OS Microbacterium endophyticum. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1526412 {ECO:0000313|EMBL:MBB2974518.1, ECO:0000313|Proteomes:UP000529310}; RN [1] {ECO:0000313|EMBL:MBB2974518.1, ECO:0000313|Proteomes:UP000529310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27099 {ECO:0000313|EMBL:MBB2974518.1, RC ECO:0000313|Proteomes:UP000529310}; RA Klenk H.-P.; RT "Sequencing the genomes of 1000 actinobacteria strains."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01152}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01152}; CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000256|HAMAP- CC Rule:MF_01152}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01152}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01152}. CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000256|HAMAP- CC Rule:MF_01152}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01152}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBB2974518.1}. 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; JACHWQ010000001; MBB2974518.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7W4V0A5; -. DR Proteomes; UP000529310; Unassembled WGS sequence. 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:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:TreeGrafter. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0042026; P:protein refolding; IEA:TreeGrafter. 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 FunFam; 2.60.260.20:FF:000005; Chaperone protein dnaJ 1, mitochondrial; 1. DR FunFam; 2.10.230.10:FF:000002; Molecular chaperone DnaJ; 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 {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01152}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01152}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_01152}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01152}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01152}; KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP- KW Rule:MF_01152}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01152}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP- KW Rule:MF_01152}. FT DOMAIN 3..67 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" FT DOMAIN 127..209 FT /note="CR-type" FT /evidence="ECO:0000259|PROSITE:PS51188" FT ZN_FING 127..209 FT /note="CR-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 157 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 183 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 197 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 200 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" SQ SEQUENCE 372 AA; 39918 MW; 7071A955299DABEF CRC64; MADHYEVLGV SREATSDEIK KAYRRLARQL HPDVNPGEDA SEKFKLVTHA YDVLSDPEQR RRYDMGGDSS PFGGGGGNAN FGGFGDIFET FFGGGGQTRG ARARSRAERG QDALVRLDLE LGDVVFGVHR DLEVDTAVLC QTCEGSCCQP GTSPVTCDIC HGSGHVQRTV RSLLGNVVTN QPCATCQGYG TTIPYPCATC QGQGRVRERR TVSLDIPAGV ENGLRLQLPG SGEVGPAGGP NGDLYIEVSV APHETFSREG DDLLATIEVS MPDAILGTTT KIDSLDGSVE LDLRAGVQSG DVLTIKGRGI TPLRGSQRGD LRVGVQVVTP TRLDSKERQM IAEFAARTKA PAPRLAEFHQ GLFSKLRDRF RS //