May protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition, may functin in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity (Probable). Overexpression of eutJ and eutS in E.coli leads to multiple BMC-like structures; eutS expression alone leads to 1 BMC-like structure per cell (PubMed:27063436). Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136). Amine and polyamine degradation; ethanolamine degradation. Part of the 17-gene eut operon transcribed from a single promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12). Not required for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12). A double eutJ-eutG deletion is not required for growth in the above conditions. A double eutG-eutH deletion is not required for growth in the above conditions. Slightly attenuated in a mouse model of infection (PubMed:10464203). A non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5, no change in acetaldehyde release on EA plus vitamin B12 (PubMed:16585748). Belongs to the EutJ family.