ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.

Hypothetical protein; Pfam: UvrB/uvrC motif; SMART: C-terminal, D2-small domain, of ClpB protein; SMART: ATPases associated with a variety of cellular activities; Pfam: Clp amino terminal domain; Pfam: AAA domain (Cdc48 subfamily); Pfam: ATPase family associated with various cellular activities (AAA); PRINTS: ATP-dependent Clp protease ATP-binding subunit signature; Pfam: C-terminal, D2-small domain, of ClpB protein; Belongs to the ClpA/ClpB family.

ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

tRNase Z; SMART: Metallo-beta-lactamase superfamily; Pfam: Beta-lactamase superfamily domain.

Glutamate racemase; Provides the (R)-glutamate required for cell wall biosynthesis.

Nicotinate phosphoribosyltransferase; Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Belongs to the NAPRTase family.

ATP-dependent Clp protease proteolytic subunit 2; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.

rdgB/HAM1 family non-canonical purine NTP pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.

Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.