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Annotation rule MF_00208
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General rule information [?]

Accession MF_00208
Dates 1-JUN-2001 (Created)
21-JAN-2020 (Last updated, Version 45)
Name MurE
Scope
Bacteria
Templates P22188 (MURE_ECOLI); Q2FZP6 (MURE_STAA8); Q97PS1 (MURE_STRPN); Q9WY79 (MURE_THEMA); Q9A196 (MURE_STRP1): [Recover all]
Triggered by

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
murE

Comments [?]

case <FT:5>
Function Catalyzes 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 RHEA:23676: ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
EC 6.3.2.13
else case <FT:1>
Function Catalyzes 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 RHEA:17969: ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
EC 6.3.2.7
else
Function Catalyzes 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 Mg(2+)
Pathway Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular location Cytoplasm.
Ptm Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Similarity Belongs 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
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;
PF02875; Mur_ligase_C; 1;
PF08245; Mur_ligase_M; 1;
TIGRFAMs TIGR01085; MurE; 1;

Features [?]

From: MURE_STAA8 (Q2FZP6)
Key     From     To       Description   Tag   Condition   FTGroup
MOTIF (Optional)     406     409       L-lysine recognition motif     D-[DN]-P-[NA]  
From: MURE_ECOLI (P22188)
NP_BIND     116     122       ATP     G-T-x-G-K-[ST]-[ST]  
REGION (Optional)     44     46       UDP-MurNAc-L-Ala-D-Glu binding     H-[QRK]-[AVCT]  
REGION (Optional)     158     159       UDP-MurNAc-L-Ala-D-Glu binding     [TS]-T  
MOTIF (Optional)     414     417       Meso-diaminopimelate recognition motif     D-N-P-R  
BINDING (Optional)     27     27       UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen     L  
BINDING (Optional)     29     29       UDP-MurNAc-L-Ala-D-Glu     [ST]  
BINDING (Optional)     157     157       UDP-MurNAc-L-Ala-D-Glu     [NQ]  
BINDING     185     185       UDP-MurNAc-L-Ala-D-Glu     [ST]  
BINDING (Optional)     191     191       UDP-MurNAc-L-Ala-D-Glu     Q  
BINDING     193     193       UDP-MurNAc-L-Ala-D-Glu     R  
MOD_RES     225     225       N6-carboxylysine     K  
case <FT:5>
REGION     414     417       Meso-diaminopimelate binding     D-N-x-R  
BINDING     390     390       Meso-diaminopimelate     R  
BINDING     465     465       Meso-diaminopimelate; via carbonyl oxygen     G  
BINDING     469     469       Meso-diaminopimelate     E  
end case

Additional information [?]

Size range 427-540 amino acids
Related rules MF_00046 (MURC)
Fusion 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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