Phosphatidylserine decarboxylase proenzyme; Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer); Belongs to the phosphatidylserine decarboxylase family. PSD-A subfamily.

PFAM: GTP-binding protein, HSR1-related; KEGG: mmg:MTBMA_c04750 GTP-binding protein.

Proteasome-activating nucleotidase; ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase- [...]

Chaperone protein dnaK; Acts as a chaperone.

KEGG: mmg:MTBMA_c16510 potassium uptake protein TrkH; TIGRFAM: Potassium uptake protein TrkH; PFAM: Cation transporter.

Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.

KEGG: mth:MTH44 30S ribosomal protein S2; TIGRFAM: Ribosomal protein S2, eukaryotic/archaeal; PFAM: Ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family.

SMART: ATPase, AAA+ type, core; TIGRFAM: ATPase, AAA-type, CDC48; KEGG: mth:MTH1639 cell division control protein Cdc48; PFAM: ATPase, AAA-type, core; ATPase, AAA-type, VAT, N-terminal; Cell division protein 48, CDC48, domain 2.

Protein grpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...]