NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

Comments

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

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000033; BAB94764.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_645716.1; -.

3D structure databases

HSSP

P22188; 1E8C. [HSSP ENTRY / PDB]

ModBase

Q8NXC2.

Enzyme and pathway databases

BioCyc

SAUR196620:MW0899-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.

TIGRFAMs

TIGR01085; murE; 1.

ProtoNet

Q8NXC2.

Genome annotation databases

GeneID

1003011; -.

GenomeReviews

BA000033_GR; MW0899.

KEGG

sam:MW0899; -.

Phylogenomic databases

HOGENOM

Q8NXC2; -.

Genome annotation databases

CMR

Q8NXC2; MW0899.

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_0000101945`
`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: 54138 Da [This is the MW of the unprocessed precursor]

CRC64: CC826CE0036ADF1A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDASTLFKKV KVKRVLGSLE QQIDDITTDS RTAREGSIFV ASVGYTVDSH KFCQSVADQG 

        70         80         90        100        110        120 
CKLVVVNKEQ SLPANVTQVV VPDTLRVASI LAHTLYDYPS HQLVTFGVTG TNGKTSIATM 

       130        140        150        160        170        180 
IHLIQRKLQK NSAYLGTNGF QINETKTKGA NTTPETVSLT KKIKEAVDAG AESMTLEVSS 

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

       250        260        270        280        290        300 
DDSFSEYLRT VTPYEVFSYG IDEEAQFMAK NIQESLQGVS FDFVTPFGTY SVKSPYVGKF 

       310        320        330        340        350        360 
NISNIMAAMI AVWSKGTSLE TIIKAVENLE PVEGRLEVLD PSLPIDLIID YAHTADGMNK 

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

       430        440        450        460        470        480 
AKGATHQNYI EFDDRAEGIK HAIDIAEPGD TVVLASKGRE PYQIMPGHIK VPHRDDLIGL 

       490 
EAAYKKFGGG PVGQ

Q8NXC2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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