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Q11GS0 (MURE_CHESB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. 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:Meso_2012
OrganismChelativorans sp. (strain BNC1) [Complete proteome] [HAMAP]
Taxonomic identifier266779 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeChelativorans

Protein attributes

Sequence length483 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 HAMAP-Rule MF_00208.

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 – 483483UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012372

Regions

Nucleotide binding107 – 1137ATP Potential
Region149 – 1502UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region404 – 4074Meso-diaminopimelate binding By similarity
Motif404 – 4074Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site291UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1761UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1821UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1841UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3801Meso-diaminopimelate By similarity
Binding site4521Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4561Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2161N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11GS0 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: A34DDB6E426467D5

FASTA48351,101
        10         20         30         40         50         60 
MKLGEFADIL PLSGSIAGET TISGLASDSR RVNAGDLFFA LQGSKADGAA YAADAAGRGA 

        70         80         90        100        110        120 
VAIIARPGTV GDVGVPVIEA DDPRHVLALA SARLYGAQPA TMVAVTGTSG KTSVAAFTRQ 

       130        140        150        160        170        180 
IWEKAGLAAA SIGTTGVVAP GRDEYGELTT PDPVSLHKLL RELADAGVTH ASMEASSHGL 

       190        200        210        220        230        240 
DQRRLDGVKL AAGGFTNLGR DHMDYHPTVE HYHQSKMRLF KTLLPKGAPA VIFADDPWSE 

       250        260        270        280        290        300 
PTEKVALAAG LQLLTVGRRG TFLTIKRVEH ERHRQRTEIE HEGMIYDIML PLAGDFQVGN 

       310        320        330        340        350        360 
ALVAAGLAIS TGLPADKAVA ALEHLKGASG RLELTGTTED GAQIYVDYAH KPDALENVLQ 

       370        380        390        400        410        420 
AVRPFTTGRV IVVFGCGGDR DPGKRPIMGE IARRLADVVI VTDDNPRSEV PAEIRRAILE 

       430        440        450        460        470        480 
AVPEATEIGD RREAIRTAVA MLNSGDTLIV AGKGHEIGQE IAGTKLPFSD HEEVRRALKE 


RTA 

« Hide

References

[1]"Complete sequence of chromosome of Mesorhizobium sp. BNC1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BNC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000390 Genomic DNA. Translation: ABG63405.1.
RefSeqYP_674570.1. NC_008254.1.

3D structure databases

ProteinModelPortalQ11GS0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266779.Meso_2012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG63405; ABG63405; Meso_2012.
GeneID4182805.
KEGGmes:Meso_2012.
PATRIC21344130. VBICheSp72577_2687.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAKIAVDYA.
OrthoDBEOG6PKFCR.

Enzyme and pathway databases

BioCycCSP266779:GI09-2046-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.40.1390.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR004101. 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. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
SSF63418. SSF63418. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_CHESB
AccessionPrimary (citable) accession number: Q11GS0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: June 11, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways