ID A0A1G0M1F9_9DELT Unreviewed; 371 AA. AC A0A1G0M1F9; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 27-SEP-2017, entry version 6. 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., RA Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected RT biogeochemical processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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. CC {ECO:0000256|HAMAP-Rule:MF_01152}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC 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 CC center 2 is essential for interaction with DnaK and for DnaJ CC activity. {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 CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01152}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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 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; 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 {ECO:0000256|HAMAP-Rule:MF_01152, KW ECO:0000256|SAAS:SAAS00842232}; KW Complete proteome {ECO:0000313|Proteomes:UP000176728}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01152}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_01152}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE- KW ProRule:PRU00546, ECO:0000256|SAAS:SAAS00786429}; KW Reference proteome {ECO:0000313|Proteomes:UP000176728}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01152, KW ECO:0000256|SAAS:SAAS00786525}; KW Stress response {ECO:0000256|HAMAP-Rule:MF_01152}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE- KW ProRule:PRU00546, ECO:0000256|SAAS:SAAS00786407}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01152, ECO:0000256|PROSITE- KW ProRule:PRU00546, ECO:0000256|SAAS:SAAS00786500}. FT DOMAIN 8 73 J. {ECO:0000259|PROSITE:PS50076}. FT DOMAIN 134 212 CR-type. {ECO:0000259|PROSITE:PS51188}. FT REPEAT 147 154 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT REPEAT 164 171 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT REPEAT 186 193 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT REPEAT 200 207 CXXCXGXG motif. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT ZN_FING 134 212 CR-type. {ECO:0000256|PROSITE-ProRule: FT PRU00546}. FT METAL 147 147 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT METAL 150 150 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT METAL 164 164 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT METAL 167 167 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT METAL 186 186 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT METAL 189 189 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT METAL 200 200 Zinc 1. {ECO:0000256|HAMAP-Rule: FT MF_01152}. FT METAL 203 203 Zinc 1. {ECO:0000256|HAMAP-Rule: FT 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 //