Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding (By similarity). Prevents aggregation of substrate proteins and promotes their refolding (PubMed:15327959, PubMed:18227175, PubMed:22834700). In vitro, activity may be independent of the presence or absence of the GroES co-chaperonin or ATP (PubMed:15327959). Shows weak ATPase activity (PubMed:15327959, PubMed:21802426). Mediates association of bacteria with macrophages (PubMed:19470749, PubMed:20633027). Acts as an adhesin that binds CD43 on the host macrophage surface (PubMed:20633027). The full-length protein elicits robust pro-inflammatory responses from dendritic cells (DCs) and promotes DC maturation and antigen presentation to T-cells. DCs exposed to full-length GroEL2 induce strong antigen-specific gamma interferon (IFN-gamma), interleukin-2 (IL-2), and IL-17A cytokine responses from CD4(+) T-cells (PubMed:29133346). Recombinant extracellular protein activates expression of NF-kappa-B in immortalized human dermal endothelial cells in a TLR4-dependent, TLR2-independent manner. Activation occurs via MYD88-dependent and -independent pathways and requires TIRAP, TRIF, TRAM and MD-2 (some experiments done in mouse cells, mice do not usually catch tuberculosis) (PubMed:15809303). Cleaved, monomeric GroEL2 is biologically relevant and significantly contributes to Hip1-mediated dampening of macrophage responses during M.tuberculosis (Mtb) infection (PubMed:24830429). Within macrophage, the cleaved form is able to detach from the bacterial surface and crosses the phagosomal membrane towards mitochondria organelles where it interacts with the host stress-70 protein (HSPA9 or mortalin) and blocks macrophage apoptosis, which promotes Mtb survival in the hostile macrophage environment (PubMed:28288970). The cleaved form is poorly immunostimulatory and is unable to promote DC maturation and antigen presentation. Proteolytic cleavage of GroEL2 allows Mtb to prevent optimal DC-T-cell cross talk during infection (PubMed:29133346). ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide. Conditions that promote oligomer formation increase the ATPase activity (PubMed:22834700). Chaperone activity is fundamentally influenced by the interdomain communication, even if oligomerization and the ability to recognize the substrates are retained (PubMed:26553853). kcat for ATPase activity is 0.28 min(-1) (PubMed:15327959). kcat for ATPase activity is 0.18 min(-1) (PubMed:21802426). Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back (Probable). Also exists as lower oligomers, including monomeric, dimeric, tetrameric and heptameric forms (PubMed:15327959, PubMed:22834700, PubMed:15547284, PubMed:21802426, PubMed:24830429). Forms monomers under standard conditions but oligomerizes in the presence of high concentrations of ammonium salts and either ATP or ADP (PubMed:22834700). Interacts with the co-chaperonin GroES (By similarity). Interacts with the serine protease Hip1 (PubMed:24830429). Interacts with host CD43 (PubMed:20633027). Monomer (PubMed:24830429). Hip1-dependent proteolytic cleavage converts multimeric GroEL2 to a monomeric form (PubMed:24830429). Interacts with host mitochondrial mortalin (PubMed:28288970). Although thought of as a cytoplasmic chaperone this protein is routinely found extracellularly in the absence of cell lysis. Exits phagosomal membrane and reaches macrophage mitochondria. Induced in response to heat shock (45 degrees Celsius), pH 10, hyperosmolarity and starvation (PubMed:18227175). Repressed by WhiB1, activated by Cmr (PubMed:22464736). Each subunit is composed of an apical domain, an intermediate domain and an equatorial domain (PubMed:26553853). The two hinges that connect the equatorial and intermediate domains (EI hinge) and the apical and intermediate domains (AI hinge) play a significant role in the chaperonin activity (PubMed:26553853). The N-terminus is important in determining the oligomerization status (PubMed:22834700). Cleaved by the mycobacterial serine protease Hip1 (PubMed:24830429). Hip1-dependent cleavage of multimeric GroEL2 results in release of cleaved monomeric GroEL2 into the extracellular milieu (PubMed:24830429). Essential, it cannot be deleted. M.tuberculosis contains two copies of the groEL gene, groEL1 and groEL2. GroEL2 is probably the housekeeping chaperonin, with the GroEL1 proteins having evolved, following an ancestral gene duplication event, to take on a more specialized role or roles. When coexpressed at high levels of expression with the co-cheperonin GroES, can complement the E.coli groEL mutant. Purified 65 kDa antigen can elicit a strong delayed-type hypersensitivity reaction in experimental animals infected with M.tuberculosis. This protein is one of the major immunoreactive proteins of the mycobacteria (PubMed:3029018). It contains epitopes that are common to various species of mycobacteria (PubMed:7699930). Belongs to the chaperonin (HSP60) family.