ID   CH60_ENTAS     STANDARD;      PRT;   539 AA.
AC   O66190;
DT   30-MAY-2000 (Rel. 39, Created)
DT   30-MAY-2000 (Rel. 39, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   60 kDa chaperonin (Protein Cpn60) (groEL protein) (Fragment).
GN   Name=groL; Synonyms=groEL, mopA;
OS   Enterobacter asburiae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=61645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 6051;
RX   PubMed=12501307;
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   -!- SUBCELLULAR LOCATION: Cytoplasmic (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 as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AB008137; BAA25207.1; -.
DR   HSSP; P06139; 1JON.
DR   HAMAP; MF_00600; -; 1.
DR   InterPro; IPR001844; Chaprnin_Cpn60.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   InterPro; IPR008950; GroEL-ATPase.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
KW   ATP-binding; Chaperone.
FT   NON_TER     539    539
SQ   SEQUENCE   539 AA;  56401 MW;  8A8A5CAF9ADBDAFB CRC64;
     MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
     ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI
     DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG
     TGLEDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV
     AKAGKPLVII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV
     ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVGQIR KQIEEATSDY
     DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVDDAL HATRAAVEEG VVAGGGVALV
     RVAAKLAGLT AQNEDQNVGI KVALRAMEAP LRQIVSNAGE EPSVVTNNVK AGEGNYGYNA
     ATEEYGNMID FGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKGDAP DLXAAGMGG
//