ID   CH601_BURPS    STANDARD;      PRT;   546 AA.
AC   Q9F712; Q63RH5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   21-MAR-2006, entry version 34.
DE   60 kDa chaperonin 1 (Protein Cpn60 1) (groEL protein 1).
GN   Name=groL1; Synonyms=groEL1, mopA; OrderedLocusNames=BPSL2697;
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=28450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
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DR   EMBL; AF287633; AAG32927.1; -; Genomic_DNA.
DR   EMBL; BX571965; CAH36705.1; -; Genomic_DNA.
DR   HSSP; P06139; 1GR5.
DR   SMR; Q9F712; 2-526.
DR   GenomeReviews; BX571965_GR; BPSL2697.
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; Complete proteome; Nucleotide-binding.
FT   CHAIN         1    546       60 kDa chaperonin 1.
FT                                /FTId=PRO_0000063318.
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
//