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Q48V28 (MURE_STRPM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:M28_Spy0314
OrganismStreptococcus pyogenes serotype M28 [Complete proteome] [HAMAP]
Taxonomic identifier319700 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length481 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 – 481481UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase HAMAP MF_00208
PRO_1000012391

Regions

Nucleotide binding118 – 1247ATP Potential
Region160 – 1612UDP-MurNAc-L-Ala-D-Glu binding By similarity
Motif404 – 4074L-lysine recognition motif HAMAP MF_00208

Sites

Binding site421UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1581UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1871UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1951UDP-MurNAc-L-Ala-D-Glu By similarity

Amino acid modifications

Modified residue2291N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q48V28 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 5781A5A357EA270D

FASTA48153,569
        10         20         30         40         50         60 
MITIEQLLDI LKKDHNFREV LDADGYHYHY QGFSFERLSY DSRQVDGKTL FFAKGATFKA 

        70         80         90        100        110        120 
DYLKEAITNG LQLYISEVDY ELGIPVVLVT DIKKAMSLIA MVFYGNPQEK LKLLAFTGTK 

       130        140        150        160        170        180 
GKTTAAYFAY HMLKESYKPA MFSTMNTTLD GKTFFKSQLT TPESLDLFAM MAECVTNGMT 

       190        200        210        220        230        240 
HLIMEVSSQA YLVDRVYGLT FDVGVFLNIS PDHIGPIEHP TFEDYFYHKR LLMENSRAVV 

       250        260        270        280        290        300 
INSGMDHFSF LADQVADQEH VFYGPLSDNQ ITTSQAFSFE AKGQLAGHYD IQLIGHFNQE 

       310        320        330        340        350        360 
NAMAAGLACL RLGASLADIQ KGIAKTRVPG RMEVLTMTNH AKVFVDYAHN GDSLEKLLSV 

       370        380        390        400        410        420 
VEEHQTGKLM LILGAPGNKG ESRRADFGRV IHQHPNLTVI LTADDPNFED PEDISKEIAS 

       430        440        450        460        470        480 
HIARPVEIIS DREQAIQKAM SLCQGAKDAV IIAGKGADAY QIVKGQQVAY AGDLAIARHY 


L

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References

[1]"Genome sequence of a serotype M28 strain of group A Streptococcus: potential new insights into puerperal sepsis and bacterial disease specificity."
Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B., Lefebvre R.B., Musser J.M.
J. Infect. Dis. 192:760-770(2005) [PubMed: 16088825] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS6180 / Serotype M28.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000056 Genomic DNA. Translation: AAX71428.1.
RefSeqYP_279783.1. NC_007296.1.

3D structure databases

ProteinModelPortalQ48V28.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000032336; EBSTRP00000031168; EBSTRG00000032336.
GeneID3574677.
GenomeReviewsGene locus M28_Spy0314 in contig CP000056_GR.
KEGGspb:M28_Spy0314.
PATRIC19743378. VBIStrPyo35950_0324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000027196.
HOGENOMHBG351099.
OMAGALAYVD.
ProtClustDBPRK14022.

Enzyme and pathway databases

BioCycSPYO319701:M28_SPY0314-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
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.
PfamPF02875. 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_STRPM
AccessionPrimary (citable) accession number: Q48V28
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 51 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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