ID A0A1G0M1F9_9DELT Unreviewed; 371 AA. AC A0A1G0M1F9; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 14-DEC-2022, entry version 25. DE RecName: Full=Chaperone protein DnaJ {ECO:0000256|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000256|HAMAP-Rule:MF_01152}; GN ORFNames=A2075_01755 {ECO:0000313|EMBL:OGU04996.1}; OS Geobacteraceae bacterium GWC2_58_44. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae. OX NCBI_TaxID=1798318 {ECO:0000313|EMBL:OGU04996.1, ECO:0000313|Proteomes:UP000176728}; RN [1] {ECO:0000313|EMBL:OGU04996.1, ECO:0000313|Proteomes:UP000176728} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27774985; DOI=10.1038/ncomms13219; RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J., RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L., RA Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected biogeochemical RT processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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: 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:OGU04996.1}. 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; MGZL01000139; OGU04996.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1G0M1F9; -. DR STRING; 1798318.A2075_01755; -. DR EnsemblBacteria; OGU04996; OGU04996; A2075_01755. DR Proteomes; UP000176728; 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: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 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; Chaperone J-domain; 1. DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1. DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2. 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 {ECO:0000256|HAMAP-Rule:MF_01152}; KW Cytoplasm {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 8..73 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" FT DOMAIN 134..212 FT /note="CR-type" FT /evidence="ECO:0000259|PROSITE:PS51188" FT REPEAT 147..154 FT /note="CXXCXGXG motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT REPEAT 164..171 FT /note="CXXCXGXG motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT REPEAT 186..193 FT /note="CXXCXGXG motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT REPEAT 200..207 FT /note="CXXCXGXG motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT ZN_FING 134..212 FT /note="CR-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546" FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 164 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" FT BINDING 167 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 189 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" 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" FT BINDING 203 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01152" SQ SEQUENCE 371 AA; 40144 MW; FF8D709910D6921E CRC64; MANGDKHDYY ELLEVNRNAS EAEIKKAYRR LAVKYHPDKN AGDKASEDKF KEVSEAYEIL SDAEKRARYD QFGHAAVGGG GFSSGGFGAG SPFGDIFGDI FGEVFGGRQK ATRGRRGDDL QYNMEVSFEE AAFGVEKKID LPYAKRCDAC GGSGAKAGTT PKTCPTCQGA GQMRFQQGFF SVSKTCSHCN GEGRVVDHPC LTCRGSGTVR DKKTISVKVP AGVETGIRLK LTGEGGQGTK GGPNGDLYVA LSVREHSLFR REDNDVVCEI PISFTQAALG CEIEVPTLDG KVNMKIPEGT QSGAVFRMRG KGIPALQGYG RGDHLVVAKV ETPTNLNRQQ RELLEELARI SGEDANPMRK NFFSKVMDLL S //