ID   CH60_BURPS     STANDARD;      PRT;   546 AA.
AC   Q9F712; Q63RH5;
DT   16-OCT-2001 (Rel. 40, Created)
DT   01-FEB-2005 (Rel. 46, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   60 kDa chaperonin (Protein Cpn60) (groEL protein).
GN   Name=groL; Synonyms=groEL, mopA; OrderedLocusNames=BPSL2697;
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=28450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Woo P.C.Y., Leung P.K.L.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L.,
RA   Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R.,
RA   Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I.,
RA   Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D.,
RA   Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K.,
RA   Keith K.E., Maddison M., Moule S., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis,
RT   Burkholderia pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; AF287633; AAG32927.1; -.
DR   EMBL; BX571965; CAH36705.1; -.
DR   HSSP; P06139; 1GR5.
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; Complete proteome.
FT   CONFLICT    428    428       G -> S (in Ref. 1).
SQ   SEQUENCE   546 AA;  57116 MW;  0DE9366EFCBD65D0 CRC64;
     MAAKDVVFGD SARAKMVEGV NILANAVKVT LGPKGRNVVL ERSFGGPTVT KDGVSVAKEI
     ELKDKLQNMG AQMVKEVASK TSDNAGDGTT TATVLAQSIV REGMKYVASG MNPMDLKRGI
     DKAVAAAVEE LKKISKPCTT NKEIAQVGAI SANSDSSIGD RIAEAMDKVG KEGVITVEDG
     KSLADELDVV EGMQFDRGYL SPYFINNPDK QVAVLENPFV LLHDKKVSNI RDLLPVLEQV
     AKAGRPLLII AEDVEGEALA TLVVNNIRGI LKTVAVKAPG FGDRRKAMLE DIAILTGGQV
     IAEETGLTLE KATLAELGQA KRIEVGKENT TIIDGAGEAV NIEARVKQIR TQIEEATSDY
     DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG IVPGGGVALI
     RARTAIAGLT GVNADQNAGI KIVLRAMEEP LRQIVTNGGE EASVVVAAVA AGKGNYGYNA
     ATGEYVDMVE AGVVDPTKVT RTALQNAASV AGLLLTTDAA VAELPKEDAP MPGGMPGGMG
     GMGMDM
//