ID S5TUE5_ENTCL Unreviewed; 546 AA. AC S5TUE5; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 19-FEB-2014, entry version 5. DE RecName: Full=60 kDa chaperonin; DE AltName: Full=GroEL protein; DE AltName: Full=Protein Cpn60; GN Name=groEL; Synonyms=groL; OS Enterobacter cloacae. OG Plasmid pECL3-NDM-1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex. OX NCBI_TaxID=550; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ECL3; PLASMID=pECL3-NDM-1; RA Wailan A.M., Sidjabat H.E., Paterson D.L.; RT "The conjugation frequency and genetic surrounding of blaNDM-1, RT blaNDM-3 and blaNDM-6 carrying plasmids in Enterobacteriaceae."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KC887917; AGS56781.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.560.10; -; 2. DR Gene3D; 3.50.7.10; -; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom. DR InterPro; IPR027413; GROEL-like_equatorial. DR PANTHER; PTHR11353; PTHR11353; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF48592; SSF48592; 2. DR SUPFAM; SSF52029; SSF52029; 1. DR TIGRFAMs; TIGR02348; GroEL; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Plasmid. SQ SEQUENCE 546 AA; 57062 MW; 4E48091CE2FC367A CRC64; MAAKDIRFGE DARSKMVRGV NVLANAVKAT LGPKGRNVVL QKSYGAPTIT KDGVSVAKEI ELADAFENMG AQMVKEVASK TSDNAGDGTT TATVLAQAFI REGMKAVAAG MNPMDLKRGI DQAVKAAVGE LKSLSKPSST SKEIAQVGAI SANSDANIGD LIAQAMDKVG KEGVITVEEG SGLDNELDVV EGMQFDRGYL SPYFVNNQQS MSADLDDPFI LLYDKKISNV RDLLPVLEGV AKAGKPLLIV AEEVEGEALA TLVVNTIRGI VKVCAVKAPG FGDRRKAMLE DMAILTGGVV ISEEVGLSLE KATIKDLGRA KKIQVSKENT TIIDGAGEGA GIEARIKQIK AQIEETSSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG IVPGGGVALI RAKAAIAGIK GVNEDQNHGI QIALRAMEAP LREIVTNAGD EPSVILNRVV EGSGAFGYNA ANGEFGDMIE FGILDPTKVT RTALQNAASI AGLMITTEAM VAEAPKKDEP AMPAGGGMGG MGGMDF //