A putative bidirectional acetate kinase that may drive flux through the ethanolamine (EA) degradation pathway under anoxic conditions found when this bacteria infects host intestine. It may generate ATP that can be used by other enzymes (EutA and EutT) in the eut pathway. Can use GTP instead of ATP with reduced efficiency (PubMed:26448059). Overexpression in E.coli yields elongated protein sheets; prevents artificial BMC formation by eutS alone or by eutK, eutL, eutM, eutN, eutS in E.coli (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). acetate + ATP = acetyl phosphate + ADP Does not need divalent cations. kcat is 545 sec(-1). 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 quadruple eutP-eutQ-eutT-eutD deletion is also not required for growth in the above conditions (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, releases slightly increased amounts of acetaldehyde on EA plus vitamin B12 (PubMed:16585748). No visible phenotype when grown on EA and tetrathionate under anoxic conditions (PubMed:26448059). Belongs to the EutP/PduV family.