HAMAP

Accession	MF_00208
Dates	1-JUN-2001 (Created) 19-MAY-2011 (Last updated, Version 37)

Data class

Protein

Predictors

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

Names

MurE

Identifier

MURE

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;

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;

Protein name

RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase; EC=6.3.2.-; AltName: Full=UDP-MurNAc-tripeptide synthetase;

Gene name

murE

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.

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.

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).

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.

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

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

GO:0005524; Molecular function: ATP binding.

GO:0008765; Molecular function: UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity.

GO:0047482; Molecular function: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity.

GO:0016881; Molecular function: acid-amino acid ligase activity.

GO:0009252; Biological process: peptidoglycan biosynthetic process.
GO:0005737; Cellular component: cytoplasm.

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

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

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]

Scope:

Bacteria

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.