M. tuberculosis GroEL

Molecular chaperones are helper proteins, which play essential roles in folding, assembly, and transport of several cellular proteins. Chaperonins, a subclass of the molecular chaperones, are homo- or hetero-oligomeric proteins, which carry out the substrate protein folding in a sequestered cavity. One of the best-characterized chaperonins is the 60-kDa chaperonin of Escherichia coli, GroEL. Chaperonins are highly conserved proteins and are known to interact with nonnative substrate proteins in an ATP-dependent manner. The E. coli genome possesses a single copy of groEL, arranged in an operonic arrangement with groES and expressed under all growth conditions. GroEL forms a cylindrical assembly with two heptameric rings and functions in coordination with the heptameric GroES.

Full Name

Mycobacterium tuberculosis GroEL

Function

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).

Biological Process

Chaperone cofactor-dependent protein refoldingManual Assertion Based On ExperimentIBA:GO_Central
DNA protectionManual Assertion Based On ExperimentIDA:MTBBASE
Nucleoid organizationManual Assertion Based On ExperimentIDA:MTBBASE
Positive regulation of transcription regulatory region DNA bindingManual Assertion Based On ExperimentIDA:CAFA
Protein foldingManual Assertion Based On ExperimentIBA:GO_Central
Protein refoldingManual Assertion Based On ExperimentIDA:CAFA
Response to heatManual Assertion Based On ExperimentIEP:MTBBASE

Cellular Location

Cytoplasm

PTM

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.