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Q182Z8 (MURE_CLOD6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:CD630_26640
OrganismClostridium difficile (strain 630) [Complete proteome] [HAMAP]
Taxonomic identifier272563 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length484 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 – 484484UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000012349

Regions

Nucleotide binding109 – 1157ATP Potential
Region151 – 1522UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region403 – 4064Meso-diaminopimelate binding By similarity
Motif403 – 4064Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1781UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3791Meso-diaminopimelate By similarity
Binding site4551Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4591Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2181N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q182Z8 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 074BC8D629034E1E

FASTA48453,908
        10         20         30         40         50         60 
MKLNDIIQGL DIINVKGELN IDINNVQYDS RKVTKGTLFI CIKGFVSDGH KYIKDAIEKG 

        70         80         90        100        110        120 
ASAFIVEEDV AIKGCTFIKV KDTRKDMAKV ADNFYNHPSQ KFNVIGVTGT NGKTSITTIL 

       130        140        150        160        170        180 
NEILTLNKNK VGLIGTIKIF DGEKDIVSNS TTPESIDLQY HFNNMLDNGC DYCAMEVSSH 

       190        200        210        220        230        240 
SLALNRVDET DFKLGIFTNL TPDHLDFHKD LEDYRKAKEK LFFKTTMANI INIDDEGGKK 

       250        260        270        280        290        300 
IYENIKGINV PCYTYGVDTK ADFMARDIKS DSDGVSYRLI TPSYEEVIFI PVPGMFTVYN 

       310        320        330        340        350        360 
TLAVIAACYV LGIPKPIYKE GLRLSNGVSG RFETVPNDKG ISVIVDYAHT PDALENVLKT 

       370        380        390        400        410        420 
TQQFAEGKII SVFGCGGDRD TEKRPLMGAI GQKYSDLCII TSDNPRTEEP EAIIKDILEG 

       430        440        450        460        470        480 
IDKKKENYHV VVDREQAIAE AISMAKKDDV VIITGKGHET YQIIGKVKHH FDDKEVANEC 


LSKM

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM180355 Genomic DNA. Translation: CAJ69550.1.
RefSeqYP_001089175.1. NC_009089.1.

3D structure databases

ProteinModelPortalQ182Z8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ182Z8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4913820.
GenomeReviewsGene locus CD2664 in contig AM180355_GR.
KEGGcdf:CD2664.
NMPDRfig|1496.1.peg.2242.
PATRIC19443803. VBICloDif38397_2788.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHBG602753.
OMAGADPYQK.
ProtClustDBPRK00139.

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_CLOD6
AccessionPrimary (citable) accession number: Q182Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: January 25, 2012
This is version 45 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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