Peptidoglycan precursor biosynthesis and lipid II export

Reviewed Escherichia coli K-12 proteins ground the conserved DAP-containing route, KT2440 representatives preserve traceability to the PSEPK pathway satisfiability audit, and reviewed Staphylococcus aureus MurE grounds the alternative L-lysine branch. MurF, MraY, and MurG use pentapeptide-generic molecular functions so the module remains valid downstream of either MurE branch; species-level gene reviews may use the corresponding stem-specific child terms. No PANTHER family or PAINT ancestral-node identifier is asserted: the checked-in family-member index does not contain most reviewed cross-species exemplars, and the shared MurE family does not distinguish DAP from L-lysine specificity. The module intentionally excludes amino-acid precursor supply, undecaprenyl-carrier synthesis and recycling, SEDS/PBP polymerization and cross-linking, and peptidoglycan remodeling. CANDIDATE ASSESSED, NOT MODELLED: the MurA-centred protein-interaction hub reported for Escherichia coli (PMID:42604454), in which MurA binds the LapB scaffold and the lipid A enzymes LpxA, LpxC, and LpxD as well as the phospholipid enzyme FabZ, is not represented here. It adds no part to this module, since MurA already occupies the enolpyruvyl-transfer step and the other five proteins catalyse no peptidoglycan-precursor reaction, and it cannot be represented as a connection either: connections are scoped to node identifiers within one module document, ModuleConnectionTypeEnum has no physical-association type, and four of the five partners (LapB, LpxA, LpxC, LpxD) are not modelled anywhere in modules/ because there is no lipid A biosynthesis module. Only FabZ is modelled, in type_ii_fatty_acid_synthesis. The finding is recorded above as an evidence item and a knowledge gap. It would become modellable if a lipid A module is created and a functional, not merely physical, consequence of the interactions is demonstrated.

Connections