ID CH60_BUCAI Reviewed; 548 AA. AC P25750; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 27-MAR-2024, entry version 136. 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}, mopA, symL; GN OrderedLocusNames=BU019; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1347769; DOI=10.1128/jb.174.6.1869-1874.1992; RA Ohtaka C., Nakamura H., Ishikawa H.; RT "Structures of chaperonins from an intracellular symbiont and their RT functional expression in Escherichia coli groE mutants."; RL J. Bacteriol. 174:1869-1874(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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; X61150; CAA43460.1; -; Genomic_DNA. DR EMBL; BA000003; BAB12746.1; -; Genomic_DNA. DR RefSeq; NP_239860.1; NC_002528.1. DR RefSeq; WP_009873980.1; NC_002528.1. DR AlphaFoldDB; P25750; -. DR SMR; P25750; -. DR STRING; 563178.BUAP5A_019; -. DR EnsemblBacteria; BAB12746; BAB12746; BAB12746. DR KEGG; buc:BU019; -. DR PATRIC; fig|107806.10.peg.31; -. DR eggNOG; COG0459; Bacteria. DR HOGENOM; CLU_016503_3_0_6; -. DR Proteomes; UP000001806; 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 3: Inferred from homology; KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..548 FT /note="Chaperonin GroEL" FT /id="PRO_0000063305" FT REGION 524..548 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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; 57911 MW; 9B33AE1E629E7592 CRC64; MAAKDVKFGN EARIKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPSIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATLLAQSIV NEGLKAVAAG MNPMDLKRGI DKAVISAVEE LKHLSVPCSD SKAITQVGTI SANADEKVGS LIAEAMEKVG NDGVITVEEG TGLQDELEVV KGMQFDRGYL SPYFINKPET GIVELENPYI LMADKKISNV REMLPILESV AKSGKPLLII SEDLEGEALA TLVVNSMRGI VKVAAVKAPG FGDRRKAMLQ DISILTGGSV ISEELAMELE KSTLEDLGQA KRVVISKDTT TIIGGVGEKH SIQSRISQIR QEIQEATSDY DKEKLNERLA KLSGGVAVLK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALV RVAGKIADLR GQNEDQNVGI RVALRAMEAP LRQIVSNSGE EPSVVTNNVK DGKGNYGYNA ATDEYGDMID FGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKEDKS SDSSSSPAGG MGGMGGMM //