Reviewed, UniProtKB/Swiss-Prot Q2FZP6 (MURE_STAA8)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
    EC=6.3.2.7
Alternative name(s):
    UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase
    L-lysine-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase

Gene names

Name:	murE
Ordered Locus Names:	SAOUHSC_00954

Organism

Staphylococcus aureus (strain NCTC 8325) [Complete proteome] [HAMAP]

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Can not use diaminopimelate as substrate. Seems to have a role in beta-lactam antibiotic resistance. Ref.2 Ref.3 Ref.4
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine. Ref.2
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208
Subcellular location	Cytoplasm By similarity.
Post-translational modification	Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity.
Miscellaneous	Expression of this protein in E.coli results in 50% incorporation of L-Lys into the peptidoglycan (which normally contains meso-diaminopimelate instead), leading to abnormal morphological changes and subsequent cell lysis. HAMAP MF_00208
Sequence similarities	Belongs to the murCDEF family. MurE subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.4 mM for UDP-N-acetylmuramoyl-L-Ala-D-Glu HAMAP MF_00208 KM=0.5 mM for L-lysine KM=0.3 mM for ATP pH dependence: Optimum pH is 8.4-9.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 493	493	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase HAMAP MF_00208		PRO_1000012382
Regions
	Nucleotide binding	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 HAMAP MF_00208
Sites
	Binding site	30	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	179	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	187	1	UDP-MurNAc-L-Ala-D-Glu By similarity
Amino acid modifications
	Modified residue	219	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2FZP6-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 0D224B23DA5A1390	FASTA	493	54,105
	10 20 30 40 50 60 MDASTLFKKV KVKRVLGSLE QQIDDITTDS RTAREGSIFV ASVGYTVDSH KFCQNVADQG 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 PVKSPYVGKF 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 PVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Enzymatic synthesis of the peptide in bacterial uridine nucleotides. III. Purification and properties of L-lysine-adding enzyme." Ito E., Strominger J.L. J. Biol. Chem. 239:210-214(1964) [PubMed: 14114846] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. Strain: Copenhagen.
[3]	"Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth." Mengin-Lecreulx D., Falla T., Blanot D., van Heijenoort J., Adams D.J., Chopra I. J. Bacteriol. 181:5909-5914(1999) [PubMed: 10498701] [Abstract] Cited for: FUNCTION.
[4]	"Role of murE in the expression of beta-lactam antibiotic resistance in Staphylococcus aureus." Gardete S., Ludovice A.M., Sobral R.G., Filipe S.R., de Lencastre H., Tomasz A. J. Bacteriol. 186:1705-1713(2004) [PubMed: 14996801] [Abstract] Cited for: ROLE IN ANTIBIOTIC RESISTANCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000253 Genomic DNA. Translation: ABD30079.1.
RefSeq	YP_499507.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3920665.
GenomeReviews	Gene locus SAOUHSC_00954 in contig CP000253_GR.
KEGG	sao:SAOUHSC_00954.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2FZP6.
OMA	Q2FZP6. HTPDGIE.
Enzyme and pathway databases
BioCyc	SAUR93061:SAOUHSC_00954-MON.
Family and domain databases
HAMAP	MF_00208. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01085. murE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_STAA8

Accession

Primary (citable) accession number: Q2FZP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 21, 2006
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)