ID CH60_SERRU Reviewed; 539 AA. AC O66202; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 02-OCT-2024, entry version 92. 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}; DE Flags: Fragment; GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600}; GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA; OS Serratia rubidaea (Serratia marinorubra). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Serratia. OX NCBI_TaxID=61652; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=JCM 1240; RX PubMed=12501307; DOI=10.2323/jgam.43.355; RA Harada H., Ishikawa H.; RT "Phylogenetical relationship based on groE genes among phenotypically RT related Enterobacter, Pantoea, Klebsiella, Serratia, and Erwinia species."; RL J. Gen. Appl. Microbiol. 43:355-361(1997). 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; AB008143; BAA25219.1; -; Genomic_DNA. DR AlphaFoldDB; O66202; -. DR SMR; O66202; -. DR STRING; 61652.AXX16_0220; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0042026; P:protein refolding; IEA:InterPro. 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 3: Inferred from homology; KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding. FT CHAIN 1..>539 FT /note="Chaperonin GroEL" FT /id="PRO_0000063526" 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 495 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600" FT NON_TER 539 SQ SEQUENCE 539 AA; 56640 MW; CE447B657515D4F0 CRC64; MAAKDVKFGN DARVKMLNGV NILADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAIV NEGLKAVAAG MNPMDLKRGI DKAVIAAVEE LKKLSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMEKVG KEGVITVEEG TGLQDELDVV EGMQFDRGYL SPYFINKPET GSVELESPFI LLADKKVSNI RELLPVLEAV AKAGKPLLIV AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTAGTV ISEEIGMELE KATLEDLGQA KRVVINKDTT IIIDGIGDEA TIQGRVAQIR QQIEEATSDY DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI RVASKIAELK GDNEDQNVGI KVALRAMEAP LRQIVINAGE EASVIANSVK AGEGSYGYNA YSEEYGDMIG MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKEDKA DMGAAGMGG //