HAMAP rule MF_00208
General rule information
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Accession | MF_00208 |
Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 49) |
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
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Identifier, protein and gene names
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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
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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 | Reaction=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; 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> | |
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 | Reaction=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; 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 | |
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 | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; |
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
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ATP-binding |
Cell cycle |
Cell division |
Cell shape |
Cell wall biogenesis/degradation |
Cytoplasm |
Ligase |
Magnesium |
Nucleotide-binding |
Peptidoglycan synthesis |
Gene Ontology
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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
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Pfam | PF01225; Mur_ligase; 1; |
Pfam | PF02875; Mur_ligase_C; 1; |
Pfam | PF08245; Mur_ligase_M; 1; |
NCBIfam | TIGR01085; MurE; 1; |
Features
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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
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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. |