Hypothetical.

GTP-binding protein in thiophene and furan oxidation; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.

Cytosol aminopeptidase (leucine aminopeptidase); Belongs to the peptidase M17 family.

ATP-dependent protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.

Cytosol aminopeptidase (leucine aminopeptidase); Belongs to the peptidase M17 family.

Oligoendopeptidase F - zinc metalloprotease.

Cytosol aminopeptidase (leucine aminopeptidase); Belongs to the peptidase M17 family.

Oligoendopeptidase F - zinc metalloprotease.

Cytosol aminopeptidase (leucine aminopeptidase); Belongs to the peptidase M17 family.

XAA-PRO aminopeptidase; Belongs to the peptidase M24B family.

Cytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis; Belongs to the cytidine and deoxycytidylate deaminase family.

XAA-PRO aminopeptidase; Belongs to the peptidase M24B family.

ATP-dependent RNA helicase.

GTP-binding protein; An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.

ATP-dependent RNA helicase.

Pseudouridine synthase (uracil hydrolase); Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family.

ATP-dependent RNA helicase.

Ribonuclease III; Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.

ATP-dependent RNA helicase.

Ribonuclease p - protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.

ATP-dependent RNA helicase.

Conserved hypothetical; Endoribonuclease that initiates mRNA decay. Belongs to the RNase Y family.

ATP-dependent RNA helicase.

Pseudouridine synthase (uracil hydrolase); Belongs to the pseudouridine synthase RluA family.

ATP-dependent RNA helicase.

GTP-binding protein in thiophene and furan oxidation; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.

ATP-dependent RNA helicase.

Virulence associated protein - Exoribonuclease; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.

Polypeptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.

Methionine aminopeptidase (map); Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

Replicative DNA helicase.

DNA polymerase I: 5'-3' exonuclease domain protein; 5'-3' exonuclease acting preferentially on double-stranded DNA.

Replicative DNA helicase.

uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.

Replicative DNA helicase.

DNA helicase II.

formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.

Endonuclease IV; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.

formamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.

DNA polymerase I: 5'-3' exonuclease domain protein; 5'-3' exonuclease acting preferentially on double-stranded DNA.