Function
Processes
Produces the D-glutamate incorporated into the second position of the peptidoglycan stem peptide.
A reusable bacterial precursor-supply module that produces D-glutamate and D-alanine from their L-enantiomers and ligates two D-alanine molecules to form D-Ala-D-Ala. These products feed the cytoplasmic Mur ligase pathway for peptidoglycan stem-peptide assembly. The module ends at free D-glutamate and D-Ala-D-Ala and excludes their incorporation by MurD and MurF, downstream lipid II synthesis, polymerization, cross-linking, D-amino-acid catabolism, periplasmic BSR metabolism, and Ldt-mediated peptidoglycan remodeling.
module.knowledge_gaps[0] · status
(0/1)module.knowledge_gaps[0].provenance[0] · reference_section_type
(0/1)module.knowledge_gaps[0].provenance[1] · reference_section_type
(0/1)✗ none found
No MODULE:d_amino_acid_cell_wall_precursor_supply deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
4 complete review(s) · 3 with deep research · 1 missing review · 1 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| ddl A0A140FWM5 | ✓ | ✓ | ✗ |
| ddlA Q88EV6 | ✓ | ✓ | ✓ |
| ddlB Q88N74 | ✓ | ✓ | ✓ |
| murI Q88PW2 | ✓ | ✓ | ✓ |
| Escherichia coli K-12 Alr P0A6B4 | ✗ | — | — |
The module is species-neutral. Exact PSEPK proteins are representative members only where current evidence supports their chemistry. The two Ddl-family variants reflect resolved PANTHER subfamilies and possible redundancy, not different reactions. A0A140FWM5 is a second PSEPK representative of the DdlB-like branch, supported by HAMAP, Rhea, domain, signature, and catalytic-site evidence despite its unreviewed status. D-glutamate and D-Ala-D-Ala converge downstream in the Mur ligase pathway but are not represented as a false linear chain.
Produces the D-glutamate incorporated into the second position of the peptidoglycan stem peptide.
Produces cytoplasmic D-alanine for D-Ala-D-Ala synthesis. A species-specific racemase is not assigned to this leaf solely from detectable in-vitro alanine racemase activity.
Ligates two D-alanine molecules to form the dipeptide used by MurF.
Ligates two D-alanine molecules to form the dipeptide used by MurF.