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.
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.

Copyright

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Cross-references

Sequence databases

EMBL

AE015929; AAO04315.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_764273.1; -.

3D structure databases

ModBase

Q8CPR2.

Enzyme and pathway databases

BioCyc

SEPI176280:SE_0718-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0047482;	Molecular function: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity (inferred from electronic annotation from EC).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from InterPro).
GO:0009252;	Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008360;	Biological process: regulation of cell shape (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00208; -; 1.
PBIL [Tree]

InterPro

IPR004101; Mur_ligase_C.
IPR013221; Mur_ligase_cen.
IPR000713; Mur_ligase_N.
IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.190.20; Mur_ligase_C; 1.
G3DSA:3.40.1190.10; Mur_ligase_cen; 1.

Pfam

PF01225; Mur_ligase; 1.
PF02875; Mur_ligase_C; 1.
PF08245; Mur_ligase_M; 1.
Pfam graphical view of domain structure.

TIGR01085; murE; 1.

Genome annotation databases

GeneID

1055759; -.

GenomeReviews

AE015929_GR; SE_0718.

KEGG

sep:SE0718; -.

Phylogenomic databases

HOGENOM

Q8CPR2; -.

Genome annotation databases

CMR

Q8CPR2; SE_0718.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 494`	`494`	`UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase.`	`PRO_0000101946`
`NP_BIND`	`110 116`	`7`	`ATP (Potential).`
`REGION`	`152 153`	`2`	`UDP-MurNAc-L-Ala-D-Glu binding (By similarity).`
`MOTIF`	`406 409`	`4`	`L-lysine recognition motif.`
`BINDING`	`30 30`		`UDP-MurNAc-L-Ala-D-Glu (By similarity).`
`BINDING`	`179 179`		`UDP-MurNAc-L-Ala-D-Glu (By similarity).`
`BINDING`	`187 187`		`UDP-MurNAc-L-Ala-D-Glu (By similarity).`
`MOD_RES`	`219 219`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 494 AA [This is the length of the unprocessed precursor]

Molecular weight: 54277 Da [This is the MW of the unprocessed precursor]

CRC64: F76DB876D7F89621 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNASALFKKI RVKNVIGTLD IQVDDITTDS RTAKEGSLFV ASKGYTVDSH KFCQNVVDQG 

        70         80         90        100        110        120 
CGIVVVNREL ELKGNVTQVV VPDTLRVASL LAHELYEFPS HQLTTYGVTG TNGKTSIATM 

       130        140        150        160        170        180 
IHLIYRKLNK NSAYLGTNGF QVNETKTKGA NTTPETVALT KKIKEAVDAN AEAMTMEVSS 

       190        200        210        220        230        240 
HGLALGRLRG VEFDVAIFSN LTQDHLDFHG TMEAYGHAKS LLFSQLGEDL SKEKYVVLNN 

       250        260        270        280        290        300 
DDDFSDYLAS VTPYEVFTYG ITHEAQFMAK NIKESLQGVE FEFCTPFGSF PVKSPYVGRF 

       310        320        330        340        350        360 
NISNIMAAMI AVWSKGTNLN EIINAVTELE PVEGRLEVLD PSLPIDLIID YAHTADGMNK 

       370        380        390        400        410        420 
LIDAVQPFVK QKLIFLVGMA GERDLTKTPE MGRVACRADY VIFTPDNPAN DDPKMLTAEL 

       430        440        450        460        470        480 
AKGATHNNYI EFDDRAEGIR HAIDIAEPGD TVVLASKGRE PYQIMPGHVK VPHRDDLIGL 

       490 
KAAYQKFGGG PLED

Q8CPR2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools