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HAMAP rule MF_00208

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_00208
Accession MF_00208
Dates 1-JUN-2001 (Created)
9-JAN-2025 (Last updated, Version 51)
Name MurE
Scope(s) Bacteria
Template(s) P22188 (MURE_ECOLI); Q2FZP6 (MURE_STAA8); Q97PS1 (MURE_STRPN); Q9WY79 (MURE_THEMA); Q9A196 (MURE_STRP1); [ Recover all ]
Triggered by HAMAP; MF_00208 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier MURE
case <FT:5>
Protein name RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase;
                 EC=6.3.2.13;
AltName: Full=Meso-A2pm-adding enzyme;
AltName: Full=Meso-diaminopimelate-adding enzyme;
AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase;
AltName: Full=UDP-MurNAc-tripeptide synthetase;
AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
else case <FT:1>
Protein name RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
                 EC=6.3.2.7;
AltName: Full=L-lysine-adding enzyme;
AltName: Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase;
AltName: Full=UDP-MurNAc-tripeptide synthetase;
AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
else
Protein name RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
                 EC=6.3.2.-;
AltName: Full=UDP-MurNAc-tripeptide synthetase;
end case
Gene name Name=murE;

Comments [?]

case <FT:5>
FUNCTIONCatalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
CATALYTIC ACTIVITY Reaction=UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6- diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma- D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+); Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13;
else case <FT:1>
FUNCTIONCatalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
CATALYTIC ACTIVITY Reaction=UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + L-lysine + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L- lysine + ADP + phosphate + H(+); Xref=Rhea:RHEA:17969, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:43474, ChEBI:CHEBI:83900, ChEBI:CHEBI:83903, ChEBI:CHEBI:456216; EC=6.3.2.7;
else
FUNCTIONCatalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
end case
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
PATHWAYCell wall biogenesis; peptidoglycan biosynthesis.
SUBCELLULAR LOCATIONCytoplasm.
PTMCarboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
SIMILARITYBelongs to the MurCDEF family. MurE subfamily.

Keywords [?]

ATP-binding
Cell cycle
Cell division
Cell shape
Cell wall biogenesis/degradation
Cytoplasm
Ligase
Magnesium
Nucleotide-binding
Peptidoglycan synthesis

Gene Ontology [?]

GO:0000287; Molecular function:magnesium ion binding
GO:0005524; Molecular function:ATP binding
case <FT:5>
GO:0008765; Molecular function:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity
else case <FT:1>
GO:0047482; Molecular function:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0016881; Molecular function:acid-amino acid ligase activity
end case
GO:0009252; Biological process:peptidoglycan biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF01225; Mur_ligase; 1;
Pfam PF02875; Mur_ligase_C; 1;
Pfam PF08245; Mur_ligase_M; 1;
NCBIfam TIGR01085; MurE; 1;

Features [?]

From: MURE_STAA8 (Q2FZP6)
Key From To Description Tag Condition FTGroup
MOTIF 406 409 /note="L-lysine recognition motif" D-[DN]-P-[NA]
From: MURE_ECOLI (P22188)
Key From To Description Tag Condition FTGroup
BINDING 116 122 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G-T-x-G-K-[ST]-[ST]
BINDING 44 46 /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- glutamate"
/ligand_id="ChEBI:CHEBI:83900"		 H-[QRK]-[AVCT]
BINDING 158 159 /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- glutamate"
/ligand_id="ChEBI:CHEBI:83900"		 [TS]-T
MOTIF 414 417 /note="Meso-diaminopimelate recognition motif" D-N-P-R
BINDING 27 27 /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- glutamate"
/ligand_id="ChEBI:CHEBI:83900"		 L
BINDING 29 29 /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- glutamate"
/ligand_id="ChEBI:CHEBI:83900"		 [ST]
BINDING 157 157 /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- glutamate"
/ligand_id="ChEBI:CHEBI:83900"		 [NQ]
BINDING 185 185 /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- glutamate"
/ligand_id="ChEBI:CHEBI:83900"		 [ST]
BINDING 191 191 /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- glutamate"
/ligand_id="ChEBI:CHEBI:83900"		 Q
BINDING 193 193 /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D- glutamate"
/ligand_id="ChEBI:CHEBI:83900"		 R
MOD_RES 225 225 /note="N6-carboxylysine" K
case <FT:5>
BINDING 414 417 /ligand="meso-2,6-diaminoheptanedioate"
/ligand_id="ChEBI:CHEBI:57791"		 D-N-x-R
BINDING 390 390 /ligand="meso-2,6-diaminoheptanedioate"
/ligand_id="ChEBI:CHEBI:57791"		 R
BINDING 465 465 /ligand="meso-2,6-diaminoheptanedioate"
/ligand_id="ChEBI:CHEBI:57791"		 G
BINDING 469 469 /ligand="meso-2,6-diaminoheptanedioate"
/ligand_id="ChEBI:CHEBI:57791"		 E
end case

Additional information [?]

Size range 427-540 amino acids
Related rules MF_00046
Fusion Nter: None Cter: 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.



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