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 01-MAY-2005 (Rel. 47, 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. RC STRAIN=LT2; RA Stephen R.J., Hinton J.C.D.; 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). CC -!- FUNCTION: Interacts with dnaK to disassemble a protein complex at CC the phage lambda origin of replication. Stimulates, jointly with CC grpE, the ATPase activity of dnaK (By similarity). CC -!- COFACTOR: Binds 2 zinc ions per monomer (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- INDUCTION: By heat shock under the control of the htpR regulatory CC protein (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; -. DR EMBL; AE008693; AAL18977.1; -. DR HSSP; P08622; 1EXK. DR StyGene; SG10620; dnaJ. DR InterPro; IPR002939; DnaJ_C. DR InterPro; IPR001305; DnaJ_CXXCXGXG. DR InterPro; IPR001623; DnaJ_N. DR InterPro; IPR008971; HSP40_DnaJ_pep. DR InterPro; IPR003095; Hsp_DnaJ. DR InterPro; IPR011031; Multihaem_cyt. 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 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 2 71 J-domain. FT DOMAIN 76 112 Gly-rich. 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 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 //