Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q819Q0 (MURE_BACCR) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BC_3914
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length491 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 – 491491UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101864

Regions

Nucleotide binding108 – 1147ATP Potential
Region150 – 1512UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region407 – 4104Meso-diaminopimelate binding By similarity
Motif407 – 4104Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1491UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1771UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3831Meso-diaminopimelate By similarity
Binding site4571Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4611Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q819Q0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: DB23525BF0B4261E

FASTA49153,713
        10         20         30         40         50         60 
MKLHTLVSCL HDFPVVPKEN PEITSIEADS RKVKEGSLFV CMKGYTVDSH DFAKQAAAQG 

        70         80         90        100        110        120 
AAAIVAERPI DVDVPVVLVK NTFRSLAVLA DYFYGQPTHK LHLIGITGTN GKTTTSHIMD 

       130        140        150        160        170        180 
EIMRAHGHKT GLIGTINMKI GDETFEVKNT TPDALTLQQT FSKMVEQGVD STVMEVSSHA 

       190        200        210        220        230        240 
LDLGRVHGCD YDVAVFTNLT QDHLDYHKTM EEYKHAKGLL FAQLGNSYNH NREKYAVLNS 

       250        260        270        280        290        300 
DDNVTEEYMR STAATVVTYG IDTTSDIMAK NIVMTSGGTT FTLVTPYESV NVTMKLIGKF 

       310        320        330        340        350        360 
NVYNVLAATA AGLVSGVKLE TIIAVIKDLA GVPGRFEVVD GGQNYTVIVD YAHTPDSLEN 

       370        380        390        400        410        420 
VLKTAKQFAK GDVYCIVGCG GDRDRTKRPI MASVATKYAT HAIYTSDNPR SEDPAAILDD 

       430        440        450        460        470        480 
MVHGASGKNY EMIIDRKEAI HHAIAKAKAD DIIIIAGKGH ETYQIIGKEV HHFDDREVAK 

       490 
EAITGRLNNE E 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP10835.1.
RefSeqNP_833634.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ819Q0.
ModBaseSearch...

Protein-protein interaction databases

STRING226900.BC3914.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP10835; AAP10835; BC_3914.
GeneID1206259.
KEGGbce:BC3914.
PATRIC32603865. VBIBacCer54481_4036.

Phylogenomic databases

eggNOGCOG0769.
KOK01928.
OMAMAKDNGA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycBCER226900:GJEU-3910-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 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. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_BACCR
AccessionPrimary (citable) accession number: Q819Q0
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