ID DNAJ_FRATU STANDARD; PRT; 371 AA. AC P48207; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE DNAJ PROTEIN. GN DNAJ. OS FRANCISELLA TULARENSIS. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC UNCERTAIN. RN [1] RP SEQUENCE FROM N.A. RA ZUBER M., HOOVER T.A., DERTZBAUGH M.T., COURT D.L.; RL SUBMITTED (JUL-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: INTERACTS WITH DNAK, TO DISASSEMBLE A PROTEIN COMPLEX CC AT THE PHAGE LAMBDA ORIGIN OF REPLICATION. STIMULATES, JOINTLY CC WITH GRPE, THE ATPASE ACTIVITY OF DNAK (BY SIMILARITY). CC -!- SIMILARITY: TO OTHER PROKARYOTIC DNAJ, AND TO EUKARYOTIC CC DNAJ-LIKE PROTEINS. 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; L43367; G893246; -. KW CHAPERONE; DNA REPLICATION; HEAT SHOCK. FT DOMAIN 3 72 DNAJ-LIKE. FT DOMAIN 79 110 GLY-RICH. FT REPEAT 140 147 CXXCXGXG MOTIF. FT REPEAT 156 163 CXXCXGXG MOTIF. FT REPEAT 178 185 CXXCXGXG MOTIF. FT REPEAT 192 199 CXXCXGXG MOTIF. SQ SEQUENCE 371 AA; 41481 MW; 01E148B1 CRC32; MQQKCYYEIL NISKTASGVE IKRAYRKLAM KYHPDRNPGD KEAEIKFKEI SEAYEILSDD SKRSRYDQFG HAGVNQQSGF GGTGGFEDIF DTFFGGGTSR GSNRSRASRG SDLEYTLEIT LEEAFFGVEK EITIPRMESC DSCDGTGSKS RSKTTCHACH GQGTIRRQQG FFAFEQTCPV CNGTGYSITD PCDACYGNGK VKKQKTLKVK IPEGVDNGDR IRLQGEGDSG SNGAMNGDLY VQIIIKEHKI FERRDINLYC EMPISFTKAC LGGDIKVPTL DGEVVLKVVP ETQTGKVFRL REKGMKSLRG HRRGDLLCKV VVETPVNLSA EQKELLEKFA DSLGEDYQSK HAPKSKTWFD NVKDYAKKFF E //