Amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the 'acetylated' ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. Similar to sprot|ARGA_YERPE (44%) and to sprot|ARGA_ECOLI (43%). Pfam (PF00696): Aspartokinase superfamily Pfam (PF00583): GCN5-related N-acetyltransferase; Specificity unclear.

Putative outer membrane lipoprotein OmlA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.

Putative stringent starvation protein B. Homology to sspB of E. coli of 38% (sprot|SSPB_ECOLI) Seems to act in concert with sspA in the regulation of several proteins during exponential and stationary-phase growth. The exact function of sspB is not yet known. Pfam: Stringent starvation protein B no signal peptide no TMHs.

Bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP; Belongs to the Ap4A hydrolase family.

50S ribosomal protein L32; Family membership; Belongs to the bacterial ribosomal protein bL32 family.

AroE protein; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).

Conserved hypothetical membrane protein; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.

Hypothetical protein, 53% identity (69% similarity) to TrEMBL;Q7NQR2. TREMBL;Q74F81. Has 2 copies of PF03976,IPR005660, Domain of unknown function (DUF344);This presumed domain is found in one or two copies per protein. The domain is about 230 amino acids in length and has many conserved motifs that are probably functionally important. No Signal Peptide or TMH present.

tRNA-nucleotidyltransferase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.