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Q8XJ99 (MURE_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. 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:CPE1862
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [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-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 – 484484UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101887

Regions

Nucleotide binding110 – 1167ATP Potential
Region152 – 1532UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region405 – 4084Meso-diaminopimelate binding By similarity
Motif405 – 4084Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site1791UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1871UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3811Meso-diaminopimelate By similarity
Binding site4551Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4591Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XJ99 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: CDB169DF3B903EB2

FASTA48454,471
        10         20         30         40         50         60 
MILKSLLKGL DYEVIKGNEE SKVQNIRYDN RKIEQGDAFV CVKGFKVDGH SFIGDAIKKG 

        70         80         90        100        110        120 
AKTLIVQEDV SVQEDITIIK VRDTRKALAI MSSNYFGNPK DKLKIIGITG TNGKTTSAFI 

       130        140        150        160        170        180 
IKSILEKAGF MTGLIGTIAN YIGNKKVDAV RTTPESYELH ELFKNMVDAG VEYCVMEVSS 

       190        200        210        220        230        240 
HSLELDRVYG IQFEEGIFTN LTRDHLDFHK TFENYYNAKF KLFERSNHSI INLDDPYGAN 

       250        260        270        280        290        300 
IVKDIEERGV KTKVSTFSIE KESDFKAFEI KSHSNGSEFK VNLEGIEEFS INIPGEYNIY 

       310        320        330        340        350        360 
NSLGCIICAY NLNIPMDKIK EGLSDVVIPG RCELVAKEKN LPYSIIIDYA HTPDGLENIL 

       370        380        390        400        410        420 
STVKAFTKNR MISVFGCGGD RDKVKRPQMG KIGCELSDIA IITSDNPRSE EPMDIINDIV 

       430        440        450        460        470        480 
KPLNYDNFVI EVNRKEAIRK AMNMALEGDV IVIAGKGHET YQILKDETIH FDEREVVYDI 


LEGK

« Hide

References

[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000016 Genomic DNA. Translation: BAB81568.1.
RefSeqNP_562778.1. NC_003366.1.

3D structure databases

ProteinModelPortalQ8XJ99.
ModBaseSearch...

Protein-protein interaction databases

STRING195102.CPE1862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB81568; BAB81568; BAB81568.
GeneID990171.
KEGGcpe:CPE1862.
PATRIC19497679. VBICloPer59675_1935.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAHTMEEYA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCPER195102:GJFM-1910-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
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_CLOPE
AccessionPrimary (citable) accession number: Q8XJ99
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 80 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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