ID CH60_ECOUT Reviewed; 548 AA. AC Q1R3B6; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600}; DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600}; DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600}; DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600}; GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}; GN OrderedLocusNames=UTI89_C4741; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UTI89 / UPEC; RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., RA Gordon J.I.; RT "Identification of genes subject to positive selection in uropathogenic RT strains of Escherichia coli: a comparative genomics approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). CC -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential CC role in assisting protein folding. The GroEL-GroES system forms a nano- CC cage that allows encapsulation of the non-native substrate proteins and CC provides a physical environment optimized to promote and accelerate CC protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00600}; CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric CC rings stacked back-to-back. Interacts with the co-chaperonin GroES. CC {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}. CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. CC {ECO:0000255|HAMAP-Rule:MF_00600}. 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; CP000243; ABE10148.1; -; Genomic_DNA. DR RefSeq; WP_000729117.1; NZ_CP064825.1. DR PDB; 2YNJ; EM; 8.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-525. DR PDB; 3E76; X-ray; 3.94 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=2-548. DR PDBsum; 2YNJ; -. DR PDBsum; 3E76; -. DR AlphaFoldDB; Q1R3B6; -. DR EMDB; EMD-2221; -. DR SMR; Q1R3B6; -. DR DIP; DIP-59993N; -. DR GeneID; 75203974; -. DR KEGG; eci:UTI89_C4741; -. DR HOGENOM; CLU_016503_3_0_6; -. DR EvolutionaryTrace; Q1R3B6; -. DR Proteomes; UP000001952; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule. DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule. DR CDD; cd03344; GroEL; 1. DR Gene3D; 3.50.7.10; GroEL; 1. DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1. DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1. DR HAMAP; MF_00600; CH60; 1. DR InterPro; IPR018370; Chaperonin_Cpn60_CS. DR InterPro; IPR001844; Cpn60/GroEL. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR NCBIfam; TIGR02348; GroEL; 1. DR PANTHER; PTHR45633; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR PANTHER; PTHR45633:SF3; 60 KDA HEAT SHOCK PROTEIN, MITOCHONDRIAL; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR PROSITE; PS00296; CHAPERONINS_CPN60; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Isomerase; KW Nucleotide-binding. FT CHAIN 1..548 FT /note="Chaperonin GroEL" FT /id="PRO_0000256909" FT BINDING 30..33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 87..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 415 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 479..481 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT BINDING 495 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" SQ SEQUENCE 548 AA; 57329 MW; CD3A0FB505F74AD1 CRC64; MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI DKAVTAAVEE LKALSVPCSD 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 //