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Reviewed, UniProtKB/Swiss-Prot Q88Y23 (MURE_LACPL)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
    EC=6.3.2.13
Alternative name(s):
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    Meso-diaminopimelate-adding enzyme
    Meso-A2pm-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase
Gene names
Name: murE
Ordered Locus Names: lp_0977
OrganismLactobacillus plantarum [Complete proteome] [HAMAP]
Taxonomic identifier1590 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

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Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the addition of meso-diaminopimelic acid 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 + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP MF_00208

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.

Sequence similarities

Belongs to the murCDEF family. MurE subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101905

Regions

Nucleotide binding110 – 1167ATP Potential
Region152 – 1532UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region410 – 4134Meso-diaminopimelate binding By similarity
Motif410 – 4134Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site321UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1511UDP-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
Binding site3861Meso-diaminopimelate By similarity
Binding site4601Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4641Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q88Y23-1 [UniParc].

Last modified April 26, 2004. Version 2.
Checksum: 456B7CA6F143C2AE

FASTA49353,810
        10         20         30         40         50         60 
MQASQLINSL KFKQVQPALT TDFDVTMLTQ DTREVQPGAM FIAVVGYHVD GHDLVDQAIE 

        70         80         90        100        110        120 
KGAKIIVASK PLDVNVPVIY VENTERAMAI LADVFYGAPS QKMRMIGVTG TNGKTTVTHL 

       130        140        150        160        170        180 
IEQIYRDQQQ ATGLIGTMYR KIKDEKLPTA NTTPDAITTQ RTLAAMRDAG VETVAMEVSS 

       190        200        210        220        230        240 
IALVLGRVWG IDYDIAVFTN LTQDHLDFHK TMAKYTEAKA MLFAQLGNKY SADGTNKVAV 

       250        260        270        280        290        300 
LNTDDPVGRE FEQYTAAHVL TFGLKPDAMI NAQNVEIKSH GTEFDLSVFG HVTHVTMQLI 

       310        320        330        340        350        360 
GQFNVYNMLA AFAAAYASGI PEDQIIKSLE KVTGVKGRFQ SVPSHTGVSV IVDYSHTPDG 

       370        380        390        400        410        420 
LLNALETIQD FATKDIYCVV GCGGDRDKTK RPKMAKIAVE HSTKPIFTSD NPRTEDPTMI 

       430        440        450        460        470        480 
LNDMVAGVPN ADVPVYEDRH VAIAKAIEAA QPGDVVLIAG KGHEDYQIIG RTKHHFDDSE 

       490 
EAAKALALKP TID

« Hide

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Cross-references

Sequence databases

AL935254 Genomic DNA. Translation: CAD63534.1. Different initiation.
RefSeqNP_784687.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1063760.
GenomeReviewsGene locus lp_0977 in contig AL935263_GR.
KEGGlpl:lp_0977.
NMPDRfig|220668.1.peg.821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ88Y23.

Enzyme and pathway databases

BioCycLPLA220668:LP_0977-MON.
BRENDA6.3.2.13. 593.

Family and domain databases

HAMAPMF_00208.
[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.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameMURE_LACPL
AccessionPrimary (citable) accession number: Q88Y23
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: June 16, 2009
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents