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Q894B7 (MURE_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. 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:CTC_01632
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length485 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 – 485485UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101888

Regions

Nucleotide binding113 – 1197ATP Potential
Region155 – 1562UDP-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 site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1821UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1901UDP-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 residue2221N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q894B7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 47F2A9B9E8A2A7AC

FASTA48554,968
        10         20         30         40         50         60 
MKLKEVLKKL EYNILNGNIE IDIENIQYDS RNIKKNDIFF AIQGYSTDGH KFIESAIEKG 

        70         80         90        100        110        120 
AKVIVFDKGF ENENMYKDIT FIKVKNSRKA LAVAASNYYG NPKDKLKLIG VTGTNGKTTS 

       130        140        150        160        170        180 
TFMIKSILEE AGFKVGLMGT ILNYIGDRKI YAQRTTPESL EIHKLFKDMV DSGVDYCVME 

       190        200        210        220        230        240 
VSSHSLYLDR VYGIEFNEGI FTNLTQDHLD FHKTFENYYN SKLMLFKNSI NSVINIDDNY 

       250        260        270        280        290        300 
GERILKEIEE KTFTYSIKKY SDLKAESVRL HSRGGEFTVD FKGNKEKINI HIPGEYNVSN 

       310        320        330        340        350        360 
ALGSILACVN EGISLKVIKR GLEKLSGVPG RCEIVTMGYN LGYDVIVDYA HTPDGLDNVL 

       370        380        390        400        410        420 
RTARDFTKGK LISVYGCGGD RDRAKRPIMG RIGTELSDLA ILTSDNPRTE EPFSIIDDIV 

       430        440        450        460        470        480 
KGVTKDNYII VQSRREAIKK AMTIAKKDDV IVVAGKGHED YQILKDKTIH FDEREVIKEI 


IEELY

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References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015927 Genomic DNA. Translation: AAO36175.1.
RefSeqNP_782238.1. NC_004557.1.

3D structure databases

ProteinModelPortalQ894B7.
ModBaseSearch...

Protein-protein interaction databases

STRING212717.CTC01632.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO36175; AAO36175; CTC_01632.
GeneID1059017.
KEGGctc:CTC01632.
PATRIC19511305. VBICloTet101274_1700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
KOK01928.
OMAHTMEEYA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCTET212717:GJAM-1505-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_CLOTE
AccessionPrimary (citable) accession number: Q894B7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 79 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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