AC MF_00208; DC Protein; auto TR HAMAP; MF_00208; -; 1; level=0 XX Names: MurE XX ID MURE case DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase; DE EC=6.3.2.13; DE AltName: Full=Meso-A2pm-adding enzyme; DE AltName: Full=Meso-diaminopimelate-adding enzyme; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase; DE AltName: Full=UDP-MurNAc-tripeptide synthetase; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase; else case DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; DE EC=6.3.2.7; DE AltName: Full=L-lysine-adding enzyme; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase; DE AltName: Full=UDP-MurNAc-tripeptide synthetase; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase; else DE RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase; DE EC=6.3.2.-; DE AltName: Full=UDP-MurNAc-tripeptide synthetase; end case GN Name=murE; XX case CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the CC nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) CC in the biosynthesis of bacterial cell-wall peptidoglycan. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D- CC muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N- CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, CC ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; CC EC=6.3.2.13; else case CC -!- FUNCTION: Catalyzes the addition of L-lysine to the nucleotide CC precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the CC biosynthesis of bacterial cell-wall peptidoglycan. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- CC glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- CC alanyl-gamma-D-glutamyl-L-lysine; Xref=Rhea:RHEA:17969, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83900, ChEBI:CHEBI:83903, CC ChEBI:CHEBI:456216; EC=6.3.2.7; else CC -!- FUNCTION: Catalyzes the addition of an amino acid to the nucleotide CC precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the CC biosynthesis of bacterial cell-wall peptidoglycan. end case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. XX DR Pfam; PF01225; Mur_ligase; 1; trigger=no DR Pfam; PF02875; Mur_ligase_C; 1; trigger=no DR Pfam; PF08245; Mur_ligase_M; 1; trigger=no DR NCBIfam; TIGR01085; MurE; 1; trigger=no XX KW ATP-binding KW Cell cycle KW Cell division KW Cell shape KW Cell wall biogenesis/degradation KW Cytoplasm KW Ligase KW Magnesium KW Nucleotide-binding KW Peptidoglycan synthesis XX GO GO:0000287; F:magnesium ion binding GO GO:0005524; F:ATP binding case GO GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity else case GO GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity else GO GO:0016881; F:acid-amino acid ligase activity end case GO GO:0009252; P:peptidoglycan biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: MURE_STAA8 (Q2FZP6) FT MOTIF 406..409 FT /note="L-lysine recognition motif" FT Optional; Condition: D-[DN]-P-[NA] FT From: MURE_ECOLI (P22188) FT BINDING 116..122 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-T-x-G-K-[ST]-[ST] FT BINDING 44..46 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT Optional; Condition: H-[QRK]-[AVCT] FT BINDING 158..159 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT Optional; Condition: [TS]-T FT MOTIF 414..417 FT /note="Meso-diaminopimelate recognition motif" FT Optional; Condition: D-N-P-R FT BINDING 27 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT Optional; Condition: L FT BINDING 29 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT Optional; Condition: [ST] FT BINDING 157 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT Optional; Condition: [NQ] FT BINDING 185 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT Condition: [ST] FT BINDING 191 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT Optional; Condition: Q FT BINDING 193 FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- FT glutamate" FT /ligand_id="ChEBI:CHEBI:83900" FT Condition: R FT MOD_RES 225 FT /note="N6-carboxylysine" FT Condition: K case FT BINDING 414..417 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT Condition: D-N-x-R FT BINDING 390 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT Condition: R FT BINDING 465 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT Condition: G FT BINDING 469 FT /ligand="meso-2,6-diaminoheptanedioate" FT /ligand_id="ChEBI:CHEBI:57791" FT Condition: E end case XX Size: 427-540; Related: MF_00046; Template: P22188; Q2FZP6; Q97PS1; Q9WY79; Q9A196; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in CLOAB, OCEIH Plasmid: None Comments: MurE catalyzes the addition of the third amino acid residue of the peptide chain of peptidoglycan. This residue, generally a diamino acid, varies among the bacterial species: meso-diaminopimelic acid (meso-A2pm) for most Gram-negative bacteria and bacilli, L-lysine for most Gram-positive bacteria, L-ornithine, meso-lanthionine, LL-A2pm, L-diaminobutyric acid, L-homoserine, etc. in particular species (PubMed=4568761). MurE is highly specific in its choice of amino acid, to ensure the presence of the specific amino acid at the third position of the pentapeptide, which is required for the lateral cross-linking that is vital for peptidoglycan integrity. MurE from Thermotoga maritima was shown to be able to add both L-lysine and D-lysine that are found in its peptidoglycan. XX # Revision 1.49 2023/06/01 //