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Q04V91 (MURE_LEPBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. 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:LBJ_0479
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira ›

Protein attributes

Sequence length500 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-Rule 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-Rule MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule 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. HAMAP-Rule MF_00208

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012370

Regions

Nucleotide binding118 – 1247ATP Potential
Region160 – 1612UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region419 – 4224Meso-diaminopimelate binding By similarity
Motif419 – 4224Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site381UDP-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
Binding site3951Meso-diaminopimelate By similarity
Binding site4711Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4751Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2271N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04V91 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 7956C64A14928D2C

FASTA50054,801
        10         20         30         40         50         60 
MKMKLTNLLH EFPELKLGSL PSGKNPDSVP IEYIQSDSRK TNPEDIFCVP ESIGTKKGEF 

        70         80         90        100        110        120 
ISNTKASVIL LHRSSNISID SSKIVLECEE DPEQLQGRIA SFLLGHPSKT LEIVAVTGTN 

       130        140        150        160        170        180 
GKTSLTNILF ALAKDQGKIC GLIGTIGVKF GDRSIDTGYT TPDASSLNLI LKQMKDEGVT 

       190        200        210        220        230        240 
TVFMEASSHG LKLGRIGGIS LKAGVFTNLT QDHLDFHSDM EDYFESKFRL FEILDVSKSP 

       250        260        270        280        290        300 
FAVLDYSSPG GNELHRKIRN NLPDLPIKAL DGIGGEYKVS NPFLTLQGTS YVLSLPGNRS 

       310        320        330        340        350        360 
QTISTNLLGS FNVRNTALAF LTGLGLGLDP KGMFSSLKEI PQIPGRFQIV YSKDRSRMAV 

       370        380        390        400        410        420 
VDYAHTPDAL ENIIRSVRNS RPKRLITLFG CGGDRDKTKR PKMARIAEEL SDQVILTSDN 

       430        440        450        460        470        480 
PRSEKPEAIL DEIQSGFSPG FTPLLREVDR ARAISEGVGI LPEGGCLLVA GKGHEEYQII 

       490        500 
GKEKRHFSDV EEVRKAFGLF

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000350 Genomic DNA. Translation: ABJ75179.1.
RefSeqYP_799937.1. NC_008510.1.

3D structure databases

ProteinModelPortalQ04V91.
ModBaseSearch...

Protein-protein interaction databases

STRING355277.LBJ_0479.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ75179; ABJ75179; LBJ_0479.
GeneID4409379.
KEGGlbj:LBJ_0479.
PATRIC22355777. VBILepBor13265_0611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAGALAYVD.
ProtClustDBCLSK574168.

Enzyme and pathway databases

BioCycLBOR355277:GHYM-768-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
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_LEPBJ
AccessionPrimary (citable) accession number: Q04V91
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: May 1, 2013
This is version 52 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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