ID DNAJ_SALTY Reviewed; 379 AA. AC P0A1G7; Q60004; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-JUN-2021, entry version 107. DE RecName: Full=Chaperone protein DnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; GN Name=dnaJ {ECO:0000255|HAMAP-Rule:MF_01152}; OrderedLocusNames=STM0013; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RA Stephen R.J., Hinton J.C.D.; RT "Salmonella typhimurium dnaK and dnaJ genes."; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). RN [3] RP ROLE IN PATHOGENICITY. RC STRAIN=x3306; RX PubMed=14977940; DOI=10.1128/iai.72.3.1364-1373.2004; RA Takaya A., Tomoyasu T., Matsui H., Yamamoto T.; RT "The DnaK/DnaJ chaperone machinery of Salmonella enterica serovar RT Typhimurium is essential for invasion of epithelial cells and survival RT within macrophages, leading to systemic infection."; RL Infect. Immun. 72:1364-1373(2004). 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 (By similarity). Necessary for invasion of epithelial cells, secretion CC of invasion proteins and proliferation within macrophages. CC {ECO:0000255|HAMAP-Rule:MF_01152, ECO:0000269|PubMed:14977940}. 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 -!- INDUCTION: By heat shock under the control of the HtpR regulatory CC protein. {ECO:0000250}. 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; U58360; AAB02911.1; -; Genomic_DNA. DR EMBL; AE006468; AAL18977.1; -; Genomic_DNA. DR RefSeq; NP_459018.1; NC_003197.2. DR RefSeq; WP_001119009.1; NC_003197.2. DR SMR; P0A1G7; -. DR PaxDb; P0A1G7; -. DR EnsemblBacteria; AAL18977; AAL18977; STM0013. DR GeneID; 1251531; -. DR KEGG; stm:STM0013; -. DR PATRIC; fig|99287.12.peg.13; -. DR HOGENOM; CLU_017633_0_7_6; -. DR OMA; SDIMDAF; -. DR PhylomeDB; P0A1G7; -. DR Proteomes; UP000001014; 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 INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..379 FT /note="Chaperone protein DnaJ" FT /id="PRO_0000070878" FT DOMAIN 5..70 FT /note="J" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT REPEAT 147..154 FT /note="CXXCXGXG motif" FT REPEAT 164..171 FT /note="CXXCXGXG motif" FT REPEAT 186..193 FT /note="CXXCXGXG motif" FT REPEAT 200..207 FT /note="CXXCXGXG motif" FT ZN_FING 134..212 FT /note="CR-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 147 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 150 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 164 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 167 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 186 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 189 FT /note="Zinc 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 200 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" FT METAL 203 FT /note="Zinc 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01152" SQ SEQUENCE 379 AA; 41313 MW; 36E6D61C729F229B CRC64; MAKRDYYEIL GVSKTAEERE IKKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDA QKRAAYDQYG HAAFEQGGMG GGFGGGFNGG ADFSDIFGDV FGDIFGGGRG RQRAARGADL RYNMDLTLEE AVRGVTKEIR IPTLEECDVC HGSGAKAGTQ PQTCPTCHGS GQVQMRQGFF AVQQTCPHCQ GRGTLIKDPC HKCHGHGRVE KSKTLSVKIP AGVDTGDRIR LAGEGEAGEH GAPAGDLYVQ VQVKQHPIFE REGNNLYCEV PINFAMAALG GEIEVPTLDG RVMLKVPSET QTGKLFRMRG KGVKSVRGGA QGDLLCRVVV ETPVGLSEKQ KQLLKDLQES FGGPTGEKNS PRSKSFFDGV KKFFDDLTR //