AC MF_00600; DC Protein; auto TR HAMAP; MF_00600; -; 1; level=0 XX Names: CH60 XX ID CH60 case not DE RecName: Full=Chaperonin GroEL; DE EC=5.6.1.7; DE AltName: Full=60 kDa chaperonin; DE AltName: Full=Chaperonin-60; DE Short=Cpn60; else case DE RecName: Full=Chaperonin GroEL, chloroplastic; DE EC=5.6.1.7; DE AltName: Full=60 kDa chaperonin; DE AltName: Full=Chaperonin-60; DE Short=Cpn60; end case GN Name=groEL; Synonyms=groL; XX 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. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an CC unfolded polypeptide.; EC=5.6.1.7; CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric CC rings stacked back-to-back. Interacts with the co-chaperonin GroES. case or CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. XX DR Pfam; PF00118; Cpn60_TCP1; 1; trigger=no DR PRINTS; PR00298; CHAPERONIN60; 1; trigger=no DR NCBIfam; TIGR02348; GroEL; 1; trigger=no DR PROSITE; PS00296; CHAPERONINS_CPN60; 1; trigger=no XX KW ATP-binding KW Chaperone case or KW Cytoplasm end case KW Isomerase KW Nucleotide-binding XX GO GO:0005524; F:ATP binding GO GO:0051082; F:unfolded protein binding GO GO:0042026; P:protein refolding case or GO GO:0005737; C:cytoplasm end case case GO GO:0009507; C:chloroplast end case XX FT From: CH60_ECOLI (P0A6F5) FT BINDING 30..33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: T-x-[GA]-P FT BINDING 87..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: D-G-T-T-T FT BINDING 479..481 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: [ND]-[AV]-[AVL] FT BINDING 51 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: K FT BINDING 415 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: G FT BINDING 495 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: D XX Size: 470-620; Related: None; Template: P0A6F5; P61491; P31293; Q60024; Scope: Bacteria Archaea; Methanococcales Archaea; Methanomicrobiales Archaea; Methanosarcinaceae Archaea; Methanospirillaceae Plastid Fusion: Nter: None Cter: None Duplicate: in ANADE, NOSS1, TRIV2, BRADU, BURO1, BURP1, BURPS, BURL3, BURTA, PARXL, CHLCV, CHLPN, CHRVO, CORDI, COREF, CORJK, CORGL, FRACC, GLOVI, CHESB, METCA, MOOTA, MYCBO, MYCLE, MYCPA, MYCTU, MYXXD, NITHX, NITWN, NOCFA, PARUW, CUTAK, PROM9, PROMA, PROMM, PROMP, PROMT, RHIEC, RHIJ3, RHILO, RHIME, RHOBA, ALBFT, RHOP2, RHOPA, RHOPB, RHORT, CERS4, RHOJR, ROSDO, SALRD, SPHAL, STRAW, STRCO, SYNAS, THEVB, SYNJA, SYNJB, SYNP6, PARMW, SYNS9, SYNSC, SYNY3, THEFY, VIBCH, VIBPA, VIBVU, VIBVY Plasmid: in ACAM1, TRIV2, ECOK1, PARDP, RHIEC, RHILO, RHIME, SINFN, SINMW Comments: None XX # Revision 1.77 2023/11/28 //