ID O66202 PRELIMINARY; PRT; 539 AA. AC O66202; DT 01-AUG-1998 (TREMBLREL. 07, CREATED) DT 01-AUG-1998 (TREMBLREL. 07, LAST SEQUENCE UPDATE) DT 01-AUG-1998 (TREMBLREL. 07, LAST ANNOTATION UPDATE) DE 60 KD CHAPERONIN (PROTEIN CPN60) (GROEL PROTEIN) DE (HEAT SHOCK PROTEIN 60) (FRAGMENT). 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.; 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 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; D1026147; -. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. KW CHAPERONE; ATP-BINDING. FT NON_TER 539 539 SQ SEQUENCE 539 AA; 56640 MW; 54D7E38A CRC32; 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 //