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Q8F4J4 (MURE_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. 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:LA_2047
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length504 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 – 504504UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101908

Regions

Nucleotide binding122 – 1287ATP Potential
Region164 – 1652UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region423 – 4264Meso-diaminopimelate binding By similarity
Motif423 – 4264Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site361UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1991UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3991Meso-diaminopimelate By similarity
Binding site4751Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4791Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2311N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8F4J4 [UniParc].

Last modified August 10, 2010. Version 2.
Checksum: 25E98C1CE2142043

FASTA50456,058
        10         20         30         40         50         60 
MKLTSLLLKF PEIKLKSFPS GKNPDSIEIE YIQSDSRKTN KNDIFCVADS IGSKKKEFIS 

        70         80         90        100        110        120 
NAKASLILLR TDSNVLNDLL EVMNSSKIFL ECEIDPEQLQ GRIASFLLGH PSKDLDIVAV 

       130        140        150        160        170        180 
TGTNGKTSLT NILFSLAKDQ GINCGLIGTI GVKFGDRVID TGYTTPDASS LNLILKEMKE 

       190        200        210        220        230        240 
EGITTVFMEA SSHGLKLGRM NGISVRAGVF TNLTQDHLDF HSDMEDYFES KFRLFEILDF 

       250        260        270        280        290        300 
SKSTFAVLDY SAPNGSKLYH KILNRFPDLL IYALDDIYRK WKISDISLNL QGTSYVLGLP 

       310        320        330        340        350        360 
GNQERKISTN LLGSFNVRNT ALAFLTGIGI GLDLEKMSNS LEKIPQIPGR FQIIYSKDRS 

       370        380        390        400        410        420 
RMAVVDYAHT PDALENIIRS VRDSQPKCLI TLFGCGGDRD RTKRPKMARI AEELSDQVIL 

       430        440        450        460        470        480 
TSDNPRTEKP ETILDEIQTG FSSGFIPLLR EVDRAKAIVE GISCLPEGGC LLVAGKGHEE 

       490        500 
YQIIGKEKRH FSDVEEVQKA FGLF 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN49246.2.
RefSeqNP_712228.2. NC_004342.2.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1151390.
GenomeReviewsGene locus LA_2047 in contig AE010300_GR.
KEGGlil:LA_2047.
PATRIC22384945. VBILepInt91350_2043.

Phylogenomic databases

HOGENOMHBG602753.
ProtClustDBCLSK574168.

Enzyme and pathway databases

BioCycLINT-130-01:LINT-130-01-001816-MONOMER.
LINT189518:LA2047-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.
KOK01928.
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_LEPIN
AccessionPrimary (citable) accession number: Q8F4J4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: August 10, 2010
Last modified: January 25, 2012
This is version 66 of the entry and version 2 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