ID CH60_SERRU STANDARD; PRT; 539 AA. AC O66202; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 60 KDA CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) (FRAGMENT). GN MOPA OR GROEL. OS Serratia rubidaea. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Serratia. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=JCM 1240; RA Harada H., Ishikawa H.; RT "Phylogenetical relationship based on groE genes among phenotypically RT related Enterobacter, Pantoea, Klebsiella, Serratia, and Erwinia RT species."; RL J. Gen. Appl. Microbiol. 43:355-361(1997). CC -!- FUNCTION: PREVENTS MISFOLDING AND PROMOTES THE REFOLDING AND CC PROPER ASSEMBLY OF UNFOLDED POLYPEPTIDES GENERATED UNDER STRESS CC CONDITIONS (BY SIMILARITY). CC -!- SUBUNIT: OLIGOMER OF 14 SUBUNITS COMPOSED OF TWO STACKED RINGS OF CC 7 SUBUNITS (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CHAPERONIN (HSP60) FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; AB008143; BAA25219.1; -. DR INTERPRO; IPR001844; -. DR INTERPRO; IPR002423; -. DR PFAM; PF00118; cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR PRINTS; PR00304; TCOMPLEXTCP1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. KW Chaperone; ATP-binding. FT NON_TER 539 539 SQ SEQUENCE 539 AA; 56640 MW; CE447B657515D4F0 CRC64; MAAKDVKFGN DARVKMLNGV NILADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI DKAVIAAVEE LKKLSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMEKVG KEGVITVEEG TGLQDELDVV EGMQFDRGYL SPYFINKPET GSVELESPFI LLADKKVSNI RELLPVLEAV AKAGKPLLIV AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTAGTV ISEEIGMELE KATLEDLGQA KRVVINKDTT IIIDGIGDEA TIQGRVAQIR QQIEEATSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI RVASKIAELK GDNEDQNVGI KVALRAMEAP LRQIVINAGE EASVIANSVK AGEGSYGYNA YSEEYGDMIG MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKEDKA DMGAAGMGG //