Prevents aggregation of substrate proteins and promotes their refolding (PubMed:15327959, PubMed:19717599, PubMed:21094166). 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:32812602). Involved in copper homeostasis (PubMed:32808291, PubMed:32812602). Binds copper and may help maintaining copper homeostasis when copper is present in excess, notably in the macrophage phagosome, by acting as a metal storage protein (PubMed:32808291, PubMed:32812602). Could be involved in copper resistance during mycobacterial biofilm formation (PubMed:32812602). Protects from copper stress in vitro (PubMed:32808291). Can also bind other metals, but binds copper with relatively higher affinity compared to nickel and cobalt (PubMed:32808291). May play an important role in survival under low aeration by affecting the expression of genes known for hypoxia response (PubMed:26822628). ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide. Oligomerization, which is mediated by phosphorylation, is required for chaperone activity. Lower oligomeric GroELs possess substrate binding activity but are inefficient in promoting refolding (PubMed:19717599). The binding of copper protects GroEL1 from destabilization and increases its ATPase activity (PubMed:32812602). kcat for ATPase activity is 0.16 min(-1). Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back (Probable). Also exists as lower oligomers, including monomeric, dimeric and heptameric forms (PubMed:15327959, PubMed:19717599, PubMed:32808291, PubMed:32812602). The switch between the single-ring (heptameric) and double-ring (tetradecameric) forms is mediated by phosphorylation on Ser-393 (PubMed:19717599). Interacts with the co-chaperonin GroES (By similarity). In response to heat shock (45 degrees Celsius) and hyperosmolarity. Each subunit is composed of an apical domain, an intermediate domain and an equatorial domain (PubMed:32808291). The apical domain is sufficient for substrate recognition (PubMed:21094166). Contains a characteristic histidine-rich C terminus which is essential for copper binding (PubMed:32808291). Copper binding causes conformational rearrangement (PubMed:32808291). Phosphorylated on Thr-25 and Thr-54 by PknF (PubMed:19201798). Phosphorylated on Ser-393 by an unknown kinase (PubMed:19717599). N-terminus is acetylated by RimI. Not essential (PubMed:18227175, PubMed:26822628). Increased heat sensitivity (at 55 degrees Celsius) (PubMed:18227175). Inactivation of the gene does not affect cell wall lipids, or growth and survival in macrophages, but mutant shows slower growth in the mouse lung and spleen in early infection and fails to produce granulomatous inflammation in either mice or guinea pigs (PubMed:18227175). This is associated with reduced cytokine expression in infected animals and macrophages (PubMed:18227175). Knockout of the gene leads to differential gene expression under low aeration stress, including down regulation of genes in copper response and genes encoding members of folate synthesis super pathway (PubMed:26822628). Survival under low aeration is significantly compromised in this knockout mutant (PubMed:26822628). Knockout mutant shows increased sensitivity to Cu(2+) (PubMed:32808291). 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. Recombinant GroEL of M.tuberculosis is unable to act as effective molecular chaperone when expressed in Escherichia coli (PubMed:18227175, PubMed:19717599, PubMed:22834700). Although M.tuberculosis GroEL1 is capable of oligomerization in its native environment, it cannot do the same in E.coli, which probably explains its lack of chaperone activity in E.coli (PubMed:19717599). Can complement M.smegmatis mutants (PubMed:22834700). Belongs to the chaperonin (HSP60) family.