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Q8NXC2 (MURE_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
EC=6.3.2.7
Alternative name(s):
L-lysine-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase
Gene names
Name:murE
Ordered Locus Names:MW0899
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP MF_00208

Catalytic activity

ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine. HAMAP MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208

Subcellular location

Cytoplasm By similarity HAMAP MF_00208.

Post-translational modification

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase HAMAP MF_00208
PRO_0000101945

Regions

Nucleotide binding110 – 1167ATP Potential
Region152 – 1532UDP-MurNAc-L-Ala-D-Glu binding By similarity
Motif406 – 4094L-lysine recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1791UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1871UDP-MurNAc-L-Ala-D-Glu By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NXC2 [UniParc].

Last modified October 19, 2002. Version 1.
Checksum: CC826CE0036ADF1A

FASTA49454,138
        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

« Hide

References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
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.
Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000033 Genomic DNA. Translation: BAB94764.1.
RefSeqNP_645716.1. NC_003923.1.

3D structure databases

ProteinModelPortalQ8NXC2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8NXC2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000026291; EBSTAP00000025330; EBSTAG00000026290.
GeneID1003011.
GenomeReviewsGene locus MW0899 in contig BA000033_GR.
KEGGsam:MW0899.
PATRIC19568367. VBIStaAur44266_0945.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
GeneTreeEBGT00050000023808.
HOGENOMHBG602753.
OMAGALAYVD.
PhylomeDBQ8NXC2.
ProtClustDBPRK14022.

Enzyme and pathway databases

BioCycSAUR196620:MW0899-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
Gene3DG3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KOK05362.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. MurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_STAAW
AccessionPrimary (citable) accession number: Q8NXC2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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