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P57815 (MURE_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. 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--2,6-diaminopimelate ligase
EC=6.3.2.13
Alternative name(s):
Meso-A2pm-adding enzyme
Meso-diaminopimelate-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase
Gene names
Name:murE
Ordered Locus Names:PM0137
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP MF_00208

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 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--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101920

Regions

Nucleotide binding113 – 1197ATP Potential
Region41 – 433UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region155 – 1562UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region410 – 4134Meso-diaminopimelate binding By similarity
Motif410 – 4134Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site241UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site261UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1541UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1821UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1901UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3861Meso-diaminopimelate By similarity
Binding site4611Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4651Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2221N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P57815 [UniParc].

Last modified April 27, 2001. Version 1.
Checksum: 6C573979606A001D

FASTA49454,171
        10         20         30         40         50         60 
MRRLTALLGQ VELAPNIELT EMILDSRAVK QGCLFVALQG HQVDGRQYIP QAIAKGASAV 

        70         80         90        100        110        120 
LAETEDAQQH LSTKIEQGVP IISFYQLGSH LSALAGLFYD NPSHKLTLVG VTGTNGKTTI 

       130        140        150        160        170        180 
SQLLAQWTTL LGHRSAVMGT IGNGLLGQVK EATNTTGSAV EVQASLADFV KRGADFAAIE 

       190        200        210        220        230        240 
VSSHGLVQHR VEALAFDVAI FTNLSRDHLD YHQSMENYAL AKKRLFTELN SRHQIINADD 

       250        260        270        280        290        300 
SVGQTWLQEQ PNAVAVSCQT DFKPHQARWL KATAIQFSQK GARIQFESSW GKGELHSALI 

       310        320        330        340        350        360 
GQFNVSNLLL VFATLLSLGY DIEKLMKTVP QLTGVCGRME RLSASNQPTA IVDYAHTPDA 

       370        380        390        400        410        420 
LEKALQAARL HCQGKLWCVF GCGGDRDRGK RPIMAKIAEQ FADHVIVTDD NPRTESAAQI 

       430        440        450        460        470        480 
VQDILAGFEH PQHVEVCHAR DQAIIQALQK ADSDDVVLIA GKGHEDYQII GTQKQHFSDQ 

       490 
ETVQQYFKVN HHHA

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed: 11248100] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004439 Genomic DNA. Translation: AAK02221.1.
RefSeqNP_245074.1. NC_002663.1.

3D structure databases

ProteinModelPortalP57815.
SMRP57815. Positions 2-488.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1243484.
GenomeReviewsGene locus PM0137 in contig AE004439_GR.
KEGGpmu:PM0137.
NMPDRfig|272843.1.peg.137.
PATRIC22869418. VBIPasMul88067_0142.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG602753.
OMAHTTPEST.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycPMUL272843:PM0137-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.
KOK01928.
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_PASMU
AccessionPrimary (citable) accession number: P57815
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: January 25, 2012
This is version 77 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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