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 18-APR-2012, entry version 57. DE RecName: Full=Chaperone protein DnaJ; GN Name=dnaJ; OrderedLocusNames=STM0013; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90371; 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 MEDLINE=21534948; 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., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT 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 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 (By CC similarity). Necessary for invasion of epithelial cells, secretion CC of invasion proteins and proliferation within macrophages. CC -!- COFACTOR: Binds 2 zinc ions per monomer (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- INDUCTION: By heat shock under the control of the HtpR regulatory CC protein (By similarity). 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 (By similarity). CC -!- SIMILARITY: Belongs to the DnaJ family. CC -!- SIMILARITY: Contains 1 CR-type zinc finger. CC -!- SIMILARITY: Contains 1 J domain. 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_003197.1. DR ProteinModelPortal; P0A1G7; -. DR SMR; P0A1G7; 2-78, 134-212. DR PRIDE; P0A1G7; -. DR GeneID; 1251531; -. DR GenomeReviews; AE006468_GR; STM0013. DR KEGG; stm:STM0013; -. DR PATRIC; 32378287; VBISalEnt20916_0013. DR HOGENOM; HBG635315; -. DR KO; K03686; -. DR OMA; YTMELTL; -. DR ProtClustDB; PRK10767; -. DR BioCyc; STYP99287:STM0013-MONOMER; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. 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 Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1. DR Gene3D; G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 1. DR HAMAP; MF_01152; DnaJ; 1; -. DR InterPro; IPR012724; DnaJ. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001623; DnaJ_N. DR InterPro; IPR018253; Heat_shock_DnaJ_CS. DR InterPro; IPR008971; HSP40/DnaJ_pept-bd. DR InterPro; IPR003095; Hsp_DnaJ. DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom. DR PANTHER; PTHR24076:SF80; PTHR24076:SF80; 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; DnaJ_N; 1. DR SUPFAM; SSF49493; HSP40_DnaJ_pep; 2. DR SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 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; Complete proteome; Cytoplasm; DNA replication; KW Metal-binding; Reference proteome; Repeat; Stress response; Zinc; KW Zinc-finger. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 379 Chaperone protein DnaJ. FT /FTId=PRO_0000070878. FT DOMAIN 5 70 J. FT REPEAT 147 154 CXXCXGXG motif. FT REPEAT 164 171 CXXCXGXG motif. FT REPEAT 186 193 CXXCXGXG motif. FT REPEAT 200 207 CXXCXGXG motif. FT ZN_FING 134 212 CR-type. FT COMPBIAS 77 117 Gly-rich. FT METAL 147 147 Zinc 1 (By similarity). FT METAL 150 150 Zinc 1 (By similarity). FT METAL 164 164 Zinc 2 (By similarity). FT METAL 167 167 Zinc 2 (By similarity). FT METAL 186 186 Zinc 2 (By similarity). FT METAL 189 189 Zinc 2 (By similarity). FT METAL 200 200 Zinc 1 (By similarity). FT METAL 203 203 Zinc 1 (By similarity). 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 //