ID DNAJ_SALTY STANDARD; PRT; 378 AA. AC P0A1G7; Q60004; DT 01-NOV-1997 (Rel. 35, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 07-FEB-2006 (Rel. 49, Last annotation update) DE Chaperone protein dnaJ. GN Name=dnaJ; OrderedLocusNames=STM0013; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; 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 (Probable). 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 domain. 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; AE008693; AAL18977.1; -; Genomic_DNA. DR HSSP; P08622; 1EXK. DR SMR; P0A1G7; 1-75, 133-211. DR StyGene; SG10620; dnaJ. DR HAMAP; MF_01152; -; 1. DR InterPro; IPR012724; DnaJ_bact. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001305; DnaJ_CXXCXGXG. DR InterPro; IPR001623; DnaJ_N. DR InterPro; IPR003095; Hsp_DnaJ. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF01556; DnaJ_C; 1. DR Pfam; PF00684; DnaJ_CXXCXGXG; 1. DR PRINTS; PR00625; DNAJPROTEIN. DR SMART; SM00271; DnaJ; 1. DR TIGRFAMs; TIGR02349; DnaJ_bact; 1. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS00637; DNAJ_CXXCXGXG; 1. KW Chaperone; Complete proteome; DNA replication; Heat shock; KW Metal-binding; Repeat; Zinc. FT INIT_MET 0 0 By similarity. FT DOMAIN 4 69 J. FT REPEAT 146 153 CXXCXGXG motif. FT REPEAT 163 170 CXXCXGXG motif. FT REPEAT 185 192 CXXCXGXG motif. FT REPEAT 199 206 CXXCXGXG motif. FT COMPBIAS 76 116 Gly-rich. FT METAL 146 146 Zinc 1 (By similarity). FT METAL 149 149 Zinc 1 (By similarity). FT METAL 163 163 Zinc 2 (By similarity). FT METAL 166 166 Zinc 2 (By similarity). FT METAL 185 185 Zinc 2 (By similarity). FT METAL 188 188 Zinc 2 (By similarity). FT METAL 199 199 Zinc 1 (By similarity). FT METAL 202 202 Zinc 1 (By similarity). SQ SEQUENCE 378 AA; 41182 MW; 176EEC64696F30A2 CRC64; AKRDYYEILG VSKTAEEREI KKAYKRLAMK YHPDRNQGDK EAEAKFKEIK EAYEVLTDAQ KRAAYDQYGH AAFEQGGMGG GFGGGFNGGA DFSDIFGDVF GDIFGGGRGR QRAARGADLR YNMDLTLEEA VRGVTKEIRI PTLEECDVCH GSGAKAGTQP QTCPTCHGSG QVQMRQGFFA VQQTCPHCQG RGTLIKDPCH KCHGHGRVEK SKTLSVKIPA GVDTGDRIRL AGEGEAGEHG APAGDLYVQV QVKQHPIFER EGNNLYCEVP INFAMAALGG EIEVPTLDGR VMLKVPSETQ TGKLFRMRGK GVKSVRGGAQ GDLLCRVVVE TPVGLSEKQK QLLKDLQESF GGPTGEKNSP RSKSFFDGVK KFFDDLTR //