ID   CH60_ERWAP     STANDARD;      PRT;   540 AA.
AC   O66222;
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   Erwinia aphidicola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Erwinia.
OX   NCBI_TaxID=68334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IAM 14479;
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; AB008153; BAA25239.1; -.
DR   HSSP; P06139; 1GRL.
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     540    540
SQ   SEQUENCE   540 AA;  56707 MW;  B5CD54DBD39373E7 CRC64;
     MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
     ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQSII TEGLKAVAAG MNPMDLKRGI
     DQAVIAAVDE LKKLSVPCSD SKAIAQVGTI SANSDATVGE LIAQAMEKVG KEGVITVEEG
     TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV
     AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIAVLTGGTV
     ISEEIGMELE KAGLEDMGQA KRVVINKDTT IIIDGTGEEA TINGRVTQIR QQIEEATSDY
     DREKLQERVA KLAGGVAVLK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALV
     RVASKLAELR GQNEDQNVGI KVALRAMESP LRQIVSNAGE EPSVVTNNVK AGEGNYGYNA
     QTEEYGDMID FGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKGDAP DLGAGGGMGG
//