HAMAP family: MF

General rule information

Accession	MF_00208
Dates	1-JUN-2001 (Created) 26-SEP-2008 (Last updated, Version 33)

Data class

Protein

Predictors

HAMAP; MF_00208; [distribution of match scores in UniProtKB];[seed alignment for MF_00208]

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=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase;
AltName:	Full=Meso-diaminopimelate-adding enzyme;
AltName:	Full=Meso-A2pm-adding enzyme;
AltName:	Full=UDP-N-acetylmuramyl-tripeptide synthetase;
AltName:	Full=UDP-MurNAc-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=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase;
AltName:	Full=L-lysine-adding enzyme;
AltName:	Full=UDP-N-acetylmuramyl-tripeptide synthetase;
AltName:	Full=UDP-MurNAc-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 (By similarity).

CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate.

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 (By similarity).

CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine.

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 (By similarity).

end case

PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

PTM: Carbamoylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP (By similarity).

SIMILARITY: Belongs to the murCDEF family. MurE subfamily.

Cross-references

Pfam	PF01225; Mur_ligase; 1; PF02875; Mur_ligase_C; 1; PF08245; Mur_ligase_M; 1;
TIGRFAMs	TIGR01085; murE; 1;

Keywords

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

Gene Ontology

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.

Features

`From: MURE_STAA8 (Q2FZP6)`
`Key`	`From`	`To`	`Description`	`Condition`	`FTGroup`
`MOTIF (Optional)`	`406`	`409`	`L-lysine recognition motif`	`D-[DN]-P-[NA]`
`From: MURE_ECOLI (P22188)`
`NP_BIND`	`116`	`122`	`ATP (Potential)`	`G-T-x-G-K-[ST]-[ST]`
`REGION (Optional)`	`44`	`46`	`UDP-MurNAc-L-Ala-D-Glu binding (By similarity)`	`H-[QRK]-[AVCT]`
`REGION (Optional)`	`158`	`159`	`UDP-MurNAc-L-Ala-D-Glu binding (By similarity)`	`[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 (By similarity)`	`L`
`BINDING (Optional)`	`29`	`29`	`UDP-MurNAc-L-Ala-D-Glu (By similarity)`	`[ST]`
`BINDING (Optional)`	`157`	`157`	`UDP-MurNAc-L-Ala-D-Glu (By similarity)`	`[NQ]`
`BINDING`	`185`	`185`	`UDP-MurNAc-L-Ala-D-Glu (By similarity)`	`[ST]`
`BINDING (Optional)`	`191`	`191`	`UDP-MurNAc-L-Ala-D-Glu (By similarity)`	`Q`
`BINDING`	`193`	`193`	`UDP-MurNAc-L-Ala-D-Glu (By similarity)`	`R`
`MOD_RES`	`225`	`225`	`N6-carboxylysine (By similarity)`	`K`

case <FT:5>

`Key`	`From`	`To`	`Description`	`Condition`	`FTGroup`
`REGION`	`414`	`417`	`Meso-diaminopimelate binding (By similarity)`	`D-N-x-R`
`BINDING`	`390`	`390`	`Meso-diaminopimelate (By similarity)`	`R`
`BINDING`	`465`	`465`	`Meso-diaminopimelate; via carbonyl oxygen (By similarity)`	`G`
`BINDING`	`469`	`469`	`Meso-diaminopimelate (By similarity)`	`E`

end case

Additional information

Size range:	427-540 amino acids
Related UniRules:	MF_00046 (MURC)
Template:	P22188 (MURE_ECOLI); Q2FZP6 (MURE_STAA8); Q97PS1 (MURE_STRPN); Q9WY79 (MURE_THEMA); Q9A196 (MURE_STRP1): [Recover all]

case <Property:PEPTIDOGL_BS>

Scope:

Bacteria

end case

Fusion:	Nter: None; Cter: None
Duplicate:	in CLOAB, OCEIH
Plasmid encoded:	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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