ID   CH60_ENTAS     STANDARD;      PRT;   539 AA.
AC   O66190;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   21-MAR-2006, entry version 34.
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; Enterobacter cloacae complex.
OX   NCBI_TaxID=61645;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB008137; BAA25207.1; -; Genomic_DNA.
DR   HSSP; P06139; 1JON.
DR   SMR; O66190; 2-526.
DR   HAMAP; MF_00600; -; 1.
DR   InterPro; IPR001844; Chaprnin_Cpn60.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   InterPro; IPR012723; GroEL.
DR   InterPro; IPR008950; GroEL-ATPase.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN         1   >539       60 kDa chaperonin.
FT                                /FTId=PRO_0000063370.
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
//