![]() |
|
Annotation rule MF_00208 |
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 |
Identifier |
|
Protein name |
|
Protein name |
|
Protein name |
|
Gene name |
|
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 |
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 |
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. |
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. |
Pfam | PF01225; Mur_ligase; 1; |
PF02875; Mur_ligase_C; 1; | |
PF08245; Mur_ligase_M; 1; | |
TIGRFAMs | TIGR01085; MurE; 1; |
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 |
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 |
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. |