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Q97PS1 (MURE_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. 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:SP_1530
OrganismStreptococcus pneumoniae [Complete proteome] [HAMAP]
Taxonomic identifier1313 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.2

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_0000101953

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 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
Q97PS1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: E4374546215FBE97

FASTA48153,731
        10         20         30         40         50         60 
MIKIETVLDI LKKDGLFREI IDQGHYHYNY SKVIFDSISY DSRKVTEDTL FFAKGAAFKK 

        70         80         90        100        110        120 
EYLLSAITQG LAWYVAEKDY EVGIPVIIVN DIKKAMSLIA MEFYGNPQEK LKLLAFTGTK 

       130        140        150        160        170        180 
GKTTAAYFAY NILSQGHRPA MLSTMNTTLD GETFFKSALT TPESIDLFDM MNQAVQNDRT 

       190        200        210        220        230        240 
HLIMEVSSQA YLVKRVYGLT FDVGVFLNIS PDHIGPIEHP SFEDYFYHKR LLMEKSRAVI 

       250        260        270        280        290        300 
INSDMDHFSV LKEQVEDQDH DFYGSQFDNQ IENSKAFSFS ATGKLAGDYD IQLIGNFNQE 

       310        320        330        340        350        360 
NAVAAGLACL RLGASLEDIK KGIAATRVPG RMEVLTQKNG AKVFIDYAHN GDSLKKLINV 

       370        380        390        400        410        420 
VETHQTGKIA LVLGSTGNKG ESRRKDFGLL LNQHPEIQVF LTADDPNYED PMAIADEISS 

       430        440        450        460        470        480 
YINHPVEKIA DRQEAIKAAM AITNHELDAV IIAGKGADCY QIIQGKKESY PGDTAVAENY 


L

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. expand/collapse author list , Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.
Science 293:498-506(2001) [PubMed: 11463916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-334 / TIGR4.
[2]"Expression, purification, crystallization and preliminary characterization of uridine 5'-diphospho-N-acetylmuramoyl L-alanyl-D-glutamate:lysine ligase (MurE) from Streptococcus pneumoniae 110K/70."
Blewett A.M., Lloyd A.J., Echalier A., Fueloep V., Dowson C.G., Bugg T.D.H., Roper D.I.
Acta Crystallogr. D 60:359-361(2004) [PubMed: 14747725] [Abstract]
Cited for: FUNCTION, CRYSTALLIZATION.
Strain: 110K/70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005672 Genomic DNA. Translation: AAK75619.1.
PIRB95178.
RefSeqNP_345979.1. NC_003028.3.

3D structure databases

ProteinModelPortalQ97PS1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000025287; EBSTRP00000024379; EBSTRG00000025287.
GeneID931309.
GenomeReviewsGene locus SP_1530 in contig AE005672_GR.
KEGGspn:SP_1530.
PATRIC19707485. VBIStrPne105772_1585.
TIGRSP_1530.

Phylogenomic databases

GeneTreeEBGT00050000027196.
HOGENOMHBG351099.
OMAGALAYVD.
ProtClustDBPRK14022.

Enzyme and pathway databases

BioCycSPNE170187-1:SP_1530-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_STRPN
AccessionPrimary (citable) accession number: Q97PS1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 1, 2001
Last modified: January 25, 2012
This is version 74 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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