DNA polymerase III/DNA elongation factor III, tau and gamma subunits; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open [...]

DNA polymerase III, delta subunit; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The delta subunit is the wrench that will open the beta subunit dimer, which has been modeled to leave a gap large enough for ssDNA to pass through. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers [...]

DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. DNA bound in the ring is bent 22 degrees, in solution primed DNA is bound more tightly than dsDNA, suggesting the clamp binds both ss- and dsDNA. In a complex of DNA with this protein, alpha, epsilon and tau subunits however the DNA is only slightly bent. Coordinates protein traffic at the replicati [...]

DNA polymerase III, chi subunit; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.

DNA polymerase III, psi subunit; Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The exact function of the psi subunit is unknown.

Thymidylate kinase; Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth; Belongs to the thymidylate kinase family.

DNA polymerase III epsilon subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. Contacts both the beta sliding clamp (dnaN) and the polymerase subunit (dnaE), stabilizing their interaction.

Septation protein, ampicillin sensitivity; Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. Belongs to the transglycosylase MltG family.

4-amino-4-deoxychorismate lyase component of para-aminobenzoate synthase multienzyme complex; Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.