ID CH60_ECOL5 Reviewed; 548 AA.
AC Q0T9P8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 01-MAY-2013, entry version 45.
DE RecName: Full=60 kDa chaperonin;
DE AltName: Full=GroEL protein;
DE AltName: Full=Protein Cpn60;
GN Name=groL; Synonyms=groEL; OrderedLocusNames=ECP_4387;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG72331.1; -; Genomic_DNA.
DR RefSeq; YP_672232.1; NC_008253.1.
DR ProteinModelPortal; Q0T9P8; -.
DR SMR; Q0T9P8; 2-525.
DR STRING; 362663.ECP_4387; -.
DR PRIDE; Q0T9P8; -.
DR EnsemblBacteria; ABG72331; ABG72331; ECP_4387.
DR GeneID; 4190456; -.
DR KEGG; ecp:ECP_4387; -.
DR PATRIC; 18199715; VBIEscCol77757_4437.
DR eggNOG; COG0459; -.
DR HOGENOM; HOG000076290; -.
DR KO; K04077; -.
DR OMA; YNGVITV; -.
DR PhylomeDB; Q0T9P8; -.
DR ProtClustDB; PRK00013; -.
DR BioCyc; ECOL362663:GIY5-4429-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0042026; P:protein refolding; IEA:HAMAP.
DR HAMAP; MF_00600; CH60; 1; -.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Chaprnin_Cpn60.
DR InterPro; IPR002423; Cpn60/TCP-1.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; GroEL-ATPase; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Nucleotide-binding.
FT CHAIN 1 548 60 kDa chaperonin.
FT /FTId=PRO_0000256910.
FT MOD_RES 117 117 N6-acetyllysine (By similarity).
SQ SEQUENCE 548 AA; 57329 MW; A14A15010C983175 CRC64;
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI
DKAVAAAVEE LKTLSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG
TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV
ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY
DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI
RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA
ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG
MGGMGGMM
//
